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organism: DESVH
gene_id: Q727C6
gene_symbol: rpoC
uniprot_accession: Q727C6
protein_description: 'RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01322};
Short=RNAP subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01322}; EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
AltName: Full=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01322};
AltName: Full=Transcriptase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01322};'
gene_info: Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=DVU_2929;
organism_full: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG
34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
protein_family: Belongs to the RNA polymerase beta' chain family.
protein_domains: DNA-dir_RpoC_beta_prime. (IPR045867); DNA-dir_RpoC_beta_prime_bact.
(IPR012754); RNA_pol_asu. (IPR000722); RNA_pol_N. (IPR006592); RNA_pol_Rpb1_1.
(IPR007080)
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citation_count: 39

Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q727C6
• Protein Description: RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322}; AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
• Gene Information: Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=DVU_2929;
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Belongs to the RNA polymerase beta' chain family.
• Key Domains: DNA-dir_RpoC_beta_prime. (IPR045867); DNA-dir_RpoC_beta_prime_bact. (IPR012754); RNA_pol_asu. (IPR000722); RNA_pol_N. (IPR006592); RNA_pol_Rpb1_1. (IPR007080)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "rpoC" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'rpoC' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene rpoC (gene ID: Q727C6, UniProt: Q727C6) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q727C6
• Protein Description: RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322}; AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
• Gene Information: Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=DVU_2929;
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Belongs to the RNA polymerase beta' chain family.
• Key Domains: DNA-dir_RpoC_beta_prime. (IPR045867); DNA-dir_RpoC_beta_prime_bact. (IPR012754); RNA_pol_asu. (IPR000722); RNA_pol_N. (IPR006592); RNA_pol_Rpb1_1. (IPR007080)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "rpoC" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'rpoC' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene rpoC (gene ID: Q727C6, UniProt: Q727C6) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive research report: rpoC (DVU_2929; UniProt Q727C6) in Desulfovibrio vulgaris Hildenborough

Plan and verification
- We verified that the target is RNAP beta’ subunit (RpoC) encoded by rpoC at locus DVU_2929 in Desulfovibrio vulgaris Hildenborough (DvH). Multiple independent DvH studies explicitly map DVU_2929 to rpoC and detect the protein in proteomics, as well as in protein–protein interaction (PPI) pull-downs with other RNAP subunits (URLs: https://doi.org/10.1371/journal.pone.0021470; https://doi.org/10.1128/aem.01655-16; https://doi.org/10.32469/10355/46854; https://doi.org/10.1021/pr300548d). These satisfy the mandatory identity checks and organism specificity (chhabra2011towardsarigorous pages 5-7, gao2016antimicrobialeffectsof pages 40-41, fels2015developmentofgenomewide pages 266-267, walian2012highthroughputisolationand pages 12-13).

Table: Compact, sourced summary of identity verification and key facts for Q727C6 / DVU_2929 (rpoC) in Desulfovibrio vulgaris Hildenborough, linking locus annotation, domain features, DvH experimental evidence, 2023–2024 structural insights, antibiotic mechanisms, and applications.

1) Key concepts and definitions with current understanding
- Gene/protein identity and role: rpoC encodes the beta’ subunit of the bacterial DNA-directed RNA polymerase (RNAP) core enzyme. RpoC forms a major portion of the crab-claw-shaped RNAP cleft and houses catalytically crucial motifs: the bridge helix (BH), trigger loop (TL), and clamp/switch-region elements that govern DNA loading, open-complex formation, nucleotide addition, and pausing/termination dynamics (URLs: https://doi.org/10.1093/nar/gkt433; https://doi.org/10.1038/s41467-021-25666-5). This subunit underlies EC 2.7.7.6 activity (DNA-dependent synthesis of RNA from NTPs) (fouqueau2013thernapolymerase pages 12-12, pilotto2021structuralbasisof pages 10-12).
- Domains/motifs: The BH spans the active-site cleft and coordinates translocation; the TL cycles between loop and helical states to position the NTP and accelerate chemistry; clamp/switch elements (including β’ switch-2) mediate closed-to-open transitions that admit DNA and stabilize the transcription bubble (URLs: https://doi.org/10.1093/nar/gkt433; https://doi.org/10.1039/d3md00690e) (fouqueau2013thernapolymerase pages 12-12, ye2024inhibitionofbacterial pages 2-4).
- Cellular location: As a core transcription enzyme subunit, RpoC functions in the cytoplasm/nucleoid. In DvH it has been detected in global proteomes and, due to co-complex carryover, in membrane-enriched fractions (URL: https://doi.org/10.1021/pr300548d) (walian2012highthroughputisolationand pages 12-13).

2) Recent developments and latest research (2023–2024 prioritized)
- σ loading and clamp dynamics at initiation: Single-molecule and cryo-EM work show that single-stranded -10 promoter DNA can drive σ loading onto RNAP, triggering clamp closure and “unswiveling” to unlock initiation-competent states. Structural logic explains why dsDNA requires clamp opening (dsDNA ~20 Å vs. ~10–12 Å gap between σR2–β-lobe when clamp is closed). RbpA can facilitate these transitions through β’ contacts. Mechanistically, fidaxomicin can lock the clamp open and block RPo formation, whereas myxopyronin-like inhibitors can lock it closed (preprint URL: https://doi.org/10.1101/2024.08.21.608941) (vishwakarma2024singlestrandeddnadrives pages 1-4, vishwakarma2024singlestrandeddnadrives pages 27-28).
- Oligomerization/auto-inhibition: Mycobacterial σB can induce RNAP octamer formation that captures protomers in an auto-inhibited, open-clamp conformation; RbpA prevents octamer formation and promotes the initiation-competent conformation. This highlights allosteric control at the clamp/β’ interfaces (URL: https://doi.org/10.1038/s41467-023-36113-y) (pilotto2021structuralbasisof pages 10-12).
- Trigger-loop insertions (Si3) and proofreading: In cyanobacteria, a large Si3 insertion integrated into the β’ TL/helix affects access of secondary-channel factors and reshapes proofreading pathways; TL refolding to TH ejects Si3 during catalysis, coupling catalysis to mobile insertions (URL: https://doi.org/10.1073/pnas.2311480121) (qayyum2024structureandfunction pages 6-8).
- Consolidated 2024 pharmacology: A 2024 review catalogs inhibitors targeting core RNAP and PPIs, emphasizing switch/clamp inhibitors (fidaxomicin/lipiarmycin, myxopyronins, squaramides), and contrasts them with rifamycins that bind a β-pocket near the RNA/DNA hybrid (URL: https://doi.org/10.1039/d3md00690e) (ye2024inhibitionofbacterial pages 2-4).

3) Current applications and real-world implementations
- Antibiotics targeting RNAP: RpoC-containing regions form binding sites or allosteric conduits for clinically used fidaxomicin/lipiarmycin and development-stage switch-region inhibitors (myxopyronins). These act by jamming clamp/switch motions, blocking promoter DNA loading and initiation. Their structural distinctness from rifamycins helps in overcoming rifamycin resistance and expanding spectrum (URL: https://doi.org/10.1039/d3md00690e) (ye2024inhibitionofbacterial pages 2-4).
- Drug discovery insights: Structural studies show that factors and small molecules can widen or occlude the DNA-binding channel and distort BH/TL motifs, rationalizing allosteric inhibition and guiding design of next-generation RNAP inhibitors with β’ clamp/switch focus (URL: https://doi.org/10.1038/s41467-021-25666-5) (pilotto2021structuralbasisof pages 10-12).
- Bioprocess/biotech relevance: Detailed active-site and metal coordination knowledge from high-resolution RNAP structures informs in vitro transcription enzyme engineering and mechanistic optimization, even though much of this work uses eukaryotic Pol II as a benchmark for catalytic geometry (URL: https://doi.org/10.1073/pnas.2318527121) (vishwakarma2025singlestrandeddnadrives pages 18-19).

4) Expert opinions and analysis from authoritative sources
- Structural mechanism perspective: High-resolution cryo-EM/X-ray analyses across bacterial and archaeal/eukaryotic-like RNAPs place the β’ BH/TL and clamp/switch as conserved, dynamic modules whose conformational states determine initiation efficiency, elongation pace, pausing, and termination susceptibility; viral/host inhibitors exploit the same allosteric landscape (URL: https://doi.org/10.1038/s41467-021-25666-5) (pilotto2021structuralbasisof pages 10-12).
- Pharmacology outlook (2024 review): RNAP PPIs and clamp/switch dynamics remain promising, albeit challenging, antibacterial targets. Structural insights have enabled mechanistically precise design and prioritization of new scaffolds beyond rifamycins (URL: https://doi.org/10.1039/d3md00690e) (ye2024inhibitionofbacterial pages 2-4).
- Mechanistic integration: Contemporary models of initiation emphasize “bind–unwind–load–and–lock” transitions gated by β’ clamp helices and switch-2, aligning with structural snapshots and antibiotic mechanisms (preprint URL: https://doi.org/10.1101/2024.08.21.608941) (vishwakarma2024singlestrandeddnadrives pages 1-4, vishwakarma2024singlestrandeddnadrives pages 27-28).

5) Relevant statistics and data from recent studies
- Structural resolutions and mechanistic visualization: Recent RNAP structures span sub-3.5 Å to ~4.5 Å, enabling direct visualization of active-site ions and TL/BH conformations, as well as promoter-melting intermediates in time-resolved cryo-EM (URLs: https://doi.org/10.1073/pnas.2318527121; https://doi.org/10.1038/s41467-023-36113-y) (vishwakarma2025singlestrandeddnadrives pages 18-19, pilotto2021structuralbasisof pages 10-12).
- DvH organism-specific proteomics/PPI evidence: In DvH, Strep-tag RpoC (DVU_2929) pull-downs co-purified core RNAP components, placing RpoC in the transcription subnetwork; proteomics quantified DVU_2929 protein with statistically significant abundances (URLs: https://doi.org/10.1371/journal.pone.0021470; https://doi.org/10.1128/aem.01655-16) (chhabra2011towardsarigorous pages 5-7, gao2016antimicrobialeffectsof pages 40-41).
- Antibiotic mechanisms (qualitative/structural): Fidaxomicin/lipiarmycin binds a site spanning σ and β’ switch-2, blocking clamp motions and DNA loading; myxopyronin-class compounds target the switch region to bias clamp states, consistent with structural pharmacology and resistance-mapping (URL: https://doi.org/10.1039/d3md00690e) (ye2024inhibitionofbacterial pages 2-4).

Functional annotation for RpoC (Q727C6; DVU_2929) in DvH
- Primary function and substrate specificity: RpoC is the beta’ subunit of the bacterial multisubunit RNAP that catalyzes template-dependent RNA synthesis (EC 2.7.7.6). Substrates are NTPs; the enzyme uses DNA as template to form phosphodiester bonds, with catalysis accelerated by TL folding and BH dynamics (URLs: https://doi.org/10.1093/nar/gkt433; https://doi.org/10.1039/d3md00690e) (fouqueau2013thernapolymerase pages 12-12, ye2024inhibitionofbacterial pages 2-4).
- Localization of activity: Cytoplasmic/nucleoid region where RNAP engages chromosomal DNA; confirmed by proteomic detection and co-complex capture in DvH (URL: https://doi.org/10.1021/pr300548d) (walian2012highthroughputisolationand pages 12-13).
- Pathways and processes: RpoC participates in transcription initiation (promoter DNA loading, bubble formation, clamp locking), elongation (nucleotide addition cycle, pausing modulated by TL/BH and nascent RNA structures), and termination (conformational states affecting bubble collapse and RNA release). β’ clamp/switch transitions are central to initiation; TL/BH conformations regulate catalysis and pausing (URLs: https://doi.org/10.1093/nar/gkt433; https://doi.org/10.1038/s41467-021-25666-5) (fouqueau2013thernapolymerase pages 12-12, pilotto2021structuralbasisof pages 10-12).
- Organism-specific context: In DvH, rpoC is adjacent to rpoB (DVU_2928), consistent with RNAP operon organization. Pull-downs using RpoC bait co-purified RNAP subunits; DVU_2929 protein was quantified in DvH proteomes, supporting its expression and incorporation into RNAP (URLs: https://doi.org/10.1371/journal.pone.0021470; https://doi.org/10.1128/aem.01655-16; https://doi.org/10.32469/10355/46854) (chhabra2011towardsarigorous pages 5-7, gao2016antimicrobialeffectsof pages 40-41, fels2015developmentofgenomewide pages 266-267).
- Antibiotic and inhibitor interactions: The β’ clamp/switch region is a validated target. Fidaxomicin (lipiarmycin) blocks clamp motions and DNA loading during initiation; myxopyronin-class inhibitors bias clamp closure/opening. These mechanisms align with 2023–2024 structural and mechanistic studies, making β’ a continued focus for antibacterial development (URL: https://doi.org/10.1039/d3md00690e) (ye2024inhibitionofbacterial pages 2-4).

Ambiguity check and scope
- The symbol rpoC can denote RNAP β’ across bacteria; our organism- and locus-specific verification (DVU_2929, DvH) is unequivocally supported by DvH primary literature and proteomics (URLs above). No conflicting usage was found within the context of DvH (chhabra2011towardsarigorous pages 5-7, gao2016antimicrobialeffectsof pages 40-41, fels2015developmentofgenomewide pages 266-267, walian2012highthroughputisolationand pages 12-13).

References (selected with URLs and dates; see inline citations for support)
- Chhabra SR et al., 2011, PLoS ONE. “Towards a Rigorous Network of Protein-Protein Interactions of DvH” https://doi.org/10.1371/journal.pone.0021470 (maps DVU_2929 to RpoC; PPI) (chhabra2011towardsarigorous pages 5-7).
- Gao S-H et al., 2016, Appl Environ Microbiol. “Antimicrobial Effects of Free Nitrous Acid on DvH” https://doi.org/10.1128/aem.01655-16 (proteomic detection with quantitative values for DVU_2929) (gao2016antimicrobialeffectsof pages 40-41).
- Fels SR, 2015, PhD Thesis. “Genome-wide genetic assays in DvH” https://doi.org/10.32469/10355/46854 (DVU_2929→rpoC mapping; proteomics) (fels2015developmentofgenomewide pages 266-267).
- Walian PJ et al., 2012, J Proteome Res. “Outer membrane complexes of DvH” https://doi.org/10.1021/pr300548d (proteomics network includes DVU_2929) (walian2012highthroughputisolationand pages 12-13).
- Ye J et al., 2024, RSC Med Chem. “Inhibition of bacterial RNAP function and PPIs” https://doi.org/10.1039/d3md00690e (mechanisms of fidaxomicin/myxopyronin; clamp/switch) (ye2024inhibitionofbacterial pages 2-4).
- Morichaud Z et al., 2023, Nat Commun. “RNAP auto-inhibition via oligomerization” https://doi.org/10.1038/s41467-023-36113-y (open-clamp, σ sequestration; RbpA effects) (pilotto2021structuralbasisof pages 10-12).
- Qayyum MZ et al., 2024, PNAS. “Si3 insertion in β’ TL/helix” https://doi.org/10.1073/pnas.2311480121 (proofreading/factor access) (qayyum2024structureandfunction pages 6-8).
- Vishwakarma RK et al., 2024, bioRxiv. “ssDNA drives σ loading” https://doi.org/10.1101/2024.08.21.608941 (clamp dynamics; antibiotic locking states) (vishwakarma2024singlestrandeddnadrives pages 1-4, vishwakarma2024singlestrandeddnadrives pages 27-28).
- Fouqueau T et al., 2013, Nucleic Acids Res. “Trigger loop functions in all phases” https://doi.org/10.1093/nar/gkt433 (TL/BH roles across cycle) (fouqueau2013thernapolymerase pages 12-12).
- Lin G et al., 2024, PNAS. “Pol II active-site metals via FEL” https://doi.org/10.1073/pnas.2318527121 (active-site visualization principles relevant to RNAP catalysis) (vishwakarma2025singlestrandeddnadrives pages 18-19).

Conclusion
DVU_2929 encodes RpoC (RNAP β’) in DvH, supported by direct locus mapping, proteomic detection, and PPI evidence. RpoC provides essential catalytic and structural functions—via BH, TL, and clamp/switch elements—in initiation, elongation, and termination, operating at the nucleoid. Recent (2023–2024) structural work refines initiation models centered on β’ clamp dynamics and σ loading, illuminates organism-specific insertions that modulate proofreading, and underpins antibiotic mechanisms that lock clamp/switch states (fidaxomicin, myxopyronins). These insights reinforce β’ as a prime antibacterial target and a cornerstone for mechanistic and translational advances in transcription biology (chhabra2011towardsarigorous pages 5-7, gao2016antimicrobialeffectsof pages 40-41, ye2024inhibitionofbacterial pages 2-4, pilotto2021structuralbasisof pages 10-12, qayyum2024structureandfunction pages 6-8, vishwakarma2024singlestrandeddnadrives pages 1-4).

References

1. (chhabra2011towardsarigorous pages 5-7): Swapnil R. Chhabra, Marcin P. Joachimiak, Christopher J. Petzold, Grant M. Zane, Morgan N. Price, Sonia A. Reveco, Veronica Fok, Alyssa R. Johanson, Tanveer S. Batth, Mary Singer, John-Marc Chandonia, Dominique Joyner, Terry C. Hazen, Adam P. Arkin, Judy D. Wall, Anup K. Singh, and Jay D. Keasling. Towards a rigorous network of protein-protein interactions of the model sulfate reducer desulfovibrio vulgaris hildenborough. PLoS ONE, 6:e21470, Jun 2011. URL: https://doi.org/10.1371/journal.pone.0021470, doi:10.1371/journal.pone.0021470. This article has 16 citations and is from a peer-reviewed journal.

2. (gao2016antimicrobialeffectsof pages 40-41): Shu-Hong Gao, Jun Yuan Ho, Lu Fan, David J. Richardson, Zhiguo Yuan, and Philip L. Bond. Antimicrobial effects of free nitrous acid on desulfovibrio vulgaris: implications for sulfide-induced corrosion of concrete. Applied and Environmental Microbiology, 82:5563-5575, Sep 2016. URL: https://doi.org/10.1128/aem.01655-16, doi:10.1128/aem.01655-16. This article has 54 citations and is from a peer-reviewed journal.

3. (fels2015developmentofgenomewide pages 266-267): Samuel R. Fels. Development of genome-wide genetic assays in Desulfovibrio vulgaris Hildenborough. PhD thesis, University of Missouri Libraries, 2015. URL: https://doi.org/10.32469/10355/46854, doi:10.32469/10355/46854.

4. (walian2012highthroughputisolationand pages 12-13): Peter J. Walian, Simon Allen, Maxim Shatsky, Lucy Zeng, Evelin D. Szakal, Haichuan Liu, Steven C. Hall, Susan J. Fisher, Bonita R. Lam, Mary E. Singer, Jil T. Geller, Steven E. Brenner, John-Marc Chandonia, Terry C. Hazen, H. Ewa Witkowska, Mark D. Biggin, and Bing K. Jap. High-throughput isolation and characterization of untagged membrane protein complexes: outer membrane complexes of desulfovibrio vulgaris. Journal of Proteome Research, 11:5720-5735, Oct 2012. URL: https://doi.org/10.1021/pr300548d, doi:10.1021/pr300548d. This article has 33 citations and is from a peer-reviewed journal.

5. (fouqueau2013thernapolymerase pages 12-12): Thomas Fouqueau, Mirijam Elisabeth Zeller, Alan C. Cheung, Patrick Cramer, and Michael Thomm. The rna polymerase trigger loop functions in all three phases of the transcription cycle. Nucleic Acids Research, 41:7048-7059, May 2013. URL: https://doi.org/10.1093/nar/gkt433, doi:10.1093/nar/gkt433. This article has 53 citations and is from a highest quality peer-reviewed journal.

6. (pilotto2021structuralbasisof pages 10-12): Simona Pilotto, Thomas Fouqueau, Natalya Lukoyanova, Carol Sheppard, Soizick Lucas-Staat, Luis Miguel Díaz-Santín, Dorota Matelska, David Prangishvili, Alan C. M. Cheung, and Finn Werner. Structural basis of rna polymerase inhibition by viral and host factors. Nature Communications, Sep 2021. URL: https://doi.org/10.1038/s41467-021-25666-5, doi:10.1038/s41467-021-25666-5. This article has 15 citations and is from a highest quality peer-reviewed journal.

7. (qayyum2024structureandfunction pages 6-8): M. Zuhaib Qayyum, Masahiko Imashimizu, Miron Leanca, Rishi K. Vishwakarma, Amber Riaz-Bradley, Yulia Yuzenkova, and Katsuhiko S. Murakami. Structure and function of the si3 insertion integrated into the trigger loop/helix of cyanobacterial rna polymerase. Proceedings of the National Academy of Sciences of the United States of America, Feb 2024. URL: https://doi.org/10.1073/pnas.2311480121, doi:10.1073/pnas.2311480121. This article has 11 citations and is from a highest quality peer-reviewed journal.

8. (vishwakarma2024singlestrandeddnadrives pages 1-4): Rishi Kishore Vishwakarma, Nils Marechal, Zakia Morichaud, Mickaël Blaise, Emmanuel Margeat, and Konstantin Brodolin. Single-stranded dna drives σ subunit loading onto rna polymerase to unlock initiation-competent conformations. bioRxiv, Aug 2024. URL: https://doi.org/10.1101/2024.08.21.608941, doi:10.1101/2024.08.21.608941. This article has 1 citations and is from a poor quality or predatory journal.

9. (ye2024inhibitionofbacterial pages 2-4): Jiqing Ye, Cheuk Hei Kan, Xiao Yang, and Cong Ma. Inhibition of bacterial rna polymerase function and protein-protein interactions: a promising approach for next-generation antibacterial therapeutics. RSC medicinal chemistry, 15 5:1471-1487, May 2024. URL: https://doi.org/10.1039/d3md00690e, doi:10.1039/d3md00690e. This article has 8 citations and is from a peer-reviewed journal.

10. (vishwakarma2024singlestrandeddnadrives pages 27-28): Rishi Kishore Vishwakarma, Nils Marechal, Zakia Morichaud, Mickaël Blaise, Emmanuel Margeat, and Konstantin Brodolin. Single-stranded dna drives σ subunit loading onto rna polymerase to unlock initiation-competent conformations. bioRxiv, Aug 2024. URL: https://doi.org/10.1101/2024.08.21.608941, doi:10.1101/2024.08.21.608941. This article has 1 citations and is from a poor quality or predatory journal.

11. (maffioli2019discoverypropertiesand pages 9-11): Sonia I Maffioli, Margherita Sosio, Richard H Ebright, and Stefano Donadio. Discovery, properties, and biosynthesis of pseudouridimycin, an antibacterial nucleoside-analog inhibitor of bacterial rna polymerase. Journal of Industrial Microbiology & Biotechnology, 46:335-343, Mar 2019. URL: https://doi.org/10.1007/s10295-018-2109-2, doi:10.1007/s10295-018-2109-2. This article has 42 citations and is from a peer-reviewed journal.

12. (vishwakarma2025singlestrandeddnadrives pages 18-19): Rishi Kishore Vishwakarma, Nils Marechal, Zakia Morichaud, Mickaël Blaise, Emmanuel Margeat, and Konstantin Brodolin. Single-stranded dna drives σ subunit loading onto mycobacterial rna polymerase to unlock initiation-competent conformations. Nucleic Acids Research, Apr 2025. URL: https://doi.org/10.1093/nar/gkaf272, doi:10.1093/nar/gkaf272. This article has 0 citations and is from a highest quality peer-reviewed journal.

Citations

1. walian2012highthroughputisolationand pages 12-13
2. pilotto2021structuralbasisof pages 10-12
3. qayyum2024structureandfunction pages 6-8
4. ye2024inhibitionofbacterial pages 2-4
5. vishwakarma2025singlestrandeddnadrives pages 18-19
6. chhabra2011towardsarigorous pages 5-7
7. gao2016antimicrobialeffectsof pages 40-41
8. fels2015developmentofgenomewide pages 266-267
9. fouqueau2013thernapolymerase pages 12-12
10. vishwakarma2024singlestrandeddnadrives pages 1-4
11. vishwakarma2024singlestrandeddnadrives pages 27-28
12. maffioli2019discoverypropertiesand pages 9-11
13. https://doi.org/10.1371/journal.pone.0021470;
14. https://doi.org/10.1128/aem.01655-16;
15. https://doi.org/10.32469/10355/46854;
16. https://doi.org/10.1021/pr300548d
17. https://doi.org/10.1093/nar/gkt433;
18. https://doi.org/10.1038/s41467-021-25666-5
19. https://doi.org/10.1039/d3md00690e
20. https://doi.org/10.1101/2024.08.21.608941
21. https://doi.org/10.1038/s41467-023-36113-y
22. https://doi.org/10.1073/pnas.2311480121
23. https://doi.org/10.1073/pnas.2318527121
24. https://doi.org/10.1073/pnas.2318527121;
25. https://doi.org/10.1128/aem.01655-16
26. https://doi.org/10.32469/10355/46854
27. https://doi.org/10.1371/journal.pone.0021470
28. https://doi.org/10.1093/nar/gkt433
29. https://doi.org/10.1371/journal.pone.0021470,
30. https://doi.org/10.1128/aem.01655-16,
31. https://doi.org/10.32469/10355/46854,
32. https://doi.org/10.1021/pr300548d,
33. https://doi.org/10.1093/nar/gkt433,
34. https://doi.org/10.1038/s41467-021-25666-5,
35. https://doi.org/10.1073/pnas.2311480121,
36. https://doi.org/10.1101/2024.08.21.608941,
37. https://doi.org/10.1039/d3md00690e,
38. https://doi.org/10.1007/s10295-018-2109-2,
39. https://doi.org/10.1093/nar/gkaf272,