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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The UniProt target Q9GF35 corresponds to MatK (maturase K), a chloroplast-encoded intron maturase in the intron maturase 2 family (MatK subfamily), annotated for Thlaspi arvense (field penny-cress). The retrieved authoritative plant literature consistently uses matK to denote the plastid gene embedded in the trnK-UUU intron that encodes a group II intron maturase/splicing factor; no alternative protein with the same symbol was identified in the retrieved sources. Therefore, functional inference for the T. arvense MatK protein is best grounded in conserved land-plant MatK biology established in tobacco and other angiosperms (homology-based functional annotation) (zoschke2010anorganellarmaturase pages 1-1).
MatK is an organellar maturase: a protein derived from bacterial group II intron-encoded proteins (IEPs) that facilitates splicing (excision) of group II introns from precursor RNAs. In land plants, MatK is widely described as the sole chloroplast-encoded maturase/splicing factor retained in the plastid genome and is typically encoded within the intron of the chloroplast lysine tRNA gene trnK-UUU (zoschke2010anorganellarmaturase pages 1-1, mizrahi2022groupiiintronencoded pages 6-7).
Group II introns are catalytic RNAs that can self-splice under permissive conditions, but in plant organelles their introns are often structurally degenerate and require protein cofactors for efficient splicing in vivo. Maturases act as such cofactors, typically by binding intron RNA to stabilize the correct folded state and promote catalytic steps (barthet2020unravelingtherole pages 1-2, mizrahi2022groupiiintronencoded pages 6-7).
Plant MatK is degenerate relative to canonical bacterial IEPs: it retains the maturase “domain X” (a conserved RNA-binding/splicing-related region) and only part of the reverse transcriptase-like region, while lacking mobility-associated domains (e.g., DNA endonuclease). This domain pattern supports a specialized role in RNA splicing rather than intron mobility (barthet2020unravelingtherole pages 1-2, qu2015analysisoftargets pages 18-21).
Direct biochemical localization in transplastomic tobacco shows MatK is a chloroplast protein enriched in the soluble fraction (stroma) rather than membranes, placing its activity in the chloroplast compartment where RNA processing/splicing occurs (zoschke2010anorganellarmaturase pages 1-1, zoschke2010anorganellarmaturase pages 3-3).
Multiple lines of evidence support MatK as a trans-acting splicing cofactor for a specific set of chloroplast group IIA introns:
Across mechanistic studies, the most consistently supported MatK targets are seven chloroplast group IIA introns:
- trnK-UUU (the intron that encodes matK)
- trnA, trnI, trnV (tRNA introns)
- atpF (ATP synthase-related transcript intron)
- rpl2 (ribosomal protein transcript intron)
- rps12 intron 2 (second intron of rps12)
These targets are explicitly listed as MatK-associated and/or MatK-dependent in land-plant studies and reviews, and were reiterated in the Plant Direct biochemical study (barthet2020unravelingtherole pages 1-2, zoschke2010anorganellarmaturase pages 1-1, qu2015analysisoftargets pages 18-21).
Attempts to generate matK knockouts in tobacco plastids did not yield homoplastomic mutants, which has been interpreted as evidence that matK is essential for viability (or at least for stable plastid gene expression necessary for survival) (zoschke2010anorganellarmaturase pages 1-1, qu2015analysisoftargets pages 18-21).
MatK expression is developmentally regulated and can show strong mRNA–protein discordance:
- MatK protein abundance peaks early in development (notably around 7 days) while matK mRNA can be low at the same stage, suggesting translational regulation and/or altered protein stability (hertel2013multiplecheckpointsfor pages 8-9, zoschke2010anorganellarmaturase pages 1-1).
- RIP/qPCR-based analyses report developmentally changing MatK–RNA associations, e.g., MatK association with atpF increases ~3-fold in older (25-day) vs young (7-day) tobacco tissue, whereas association with trnV decreases ~2-fold (qu2015analysisoftargets pages 60-63).
- A quantitative modeling framework proposed negative autoregulation through pre-trnK/MatK complexes and competition among tRNA targets, consistent with multiple “checkpoints” controlling MatK abundance and interaction with intron substrates (hertel2013multiplecheckpointsfor pages 8-9).
Within the retrieved 2023–2024 corpus, there was limited accessible new mechanistic primary evidence that substantially changes the established MatK model (stroma-localized maturase acting on a conserved set of group IIA introns). The strongest mechanistic evidence in the retrieved set remains earlier high-impact work (2010–2020), including in vivo RNA association mapping and direct in vitro activity demonstration (zoschke2010anorganellarmaturase pages 1-1, barthet2020unravelingtherole pages 1-2).
Recent work continues to document matK sequence variation and rapid evolution in applied genomics contexts. For example, a 2024 study amplified a 730-bp partial matK region and reported eight variable sites across aligned Ficus species sequences, emphasizing matK’s relatively higher evolutionary rate compared with rbcL and its utility as a discriminatory plastid locus (primandiri2024thematurasek pages 1-5).
MatK’s real-world use is dominated by its role as a chloroplast DNA barcode and phylogenetic marker, distinct from its protein function as a maturase.
A 2024 field-oriented barcoding study of 91 terrestrial plant species (mostly invasive) evaluated four loci (ITS, rbcL, matK, trnH-psbA) and reported an overall PCR-and-sequencing success rate of 87.9% across loci. In that study, combining rbcL + matK yielded 68.6% species discrimination, whereas ITS + trnH-psbA achieved 97.1%, motivating a practical recommendation for dual-locus strategies emphasizing ITS + trnH-psbA over rbcL+matK in that context (nath2024dnabarcodingof pages 2-3, nath2024dnabarcodingof pages 9-10).
A 2024 Cactaceae study illustrates a common implementation issue: universal matK primers can fail in some lineages. The authors report universal matK primers had <10% amplification success, while designing lineage-specific primers increased amplification to 91.95%; nevertheless, good-quality matK sequence recovery was 54.16% (lower than rbcL 81.25% in that study). Using BLAST-based identification, matK achieved 83.33% genus-level and 50% species-level identification in their dataset (wei2024effectivenessofdna pages 3-4, wei2024effectivenessofdna pages 1-2).
A 2024 review focusing on forensic botany concluded that matK can have high recovery in some contexts (e.g., 91.8% recovery cited for one wood-forensics dataset) but can show only moderate species-level identification in others (e.g., 62.5% in a cited Paphiopedilum dataset). The review emphasizes that multi-locus combinations can substantially improve identification performance (e.g., cited 3-marker combinations averaging 91.4%, and a cited psbA-trnH + trnK combination reaching 100% in one dataset), supporting real-world practice of combining markers rather than relying on matK alone (behura2024differentdnabarcoding pages 7-9).
Recommended functional statement (protein-level): MatK is a chloroplast stromal group II intron maturase that binds and promotes splicing/excision of multiple chloroplast group IIA introns, including trnK-UUU, trnA, trnI, trnV, atpF, rpl2, and rps12 intron 2. It is likely essential for proper chloroplast RNA maturation and plastid gene expression. Evidence includes in vivo RNA association mapping and direct in vitro demonstration of maturase activity (enhanced rps12 intron 2 self-splicing) (zoschke2010anorganellarmaturase pages 1-1, barthet2020unravelingtherole pages 1-2).
| Aspect | Details | Evidence type | Key quantitative findings | Key citations with year and DOI/URL |
|---|---|---|---|---|
| Identity / genome context | MatK is the plastid-encoded maturase K relevant to UniProt Q9GF35 from Thlaspi arvense; in land plants it is typically encoded within the chloroplast trnK-UUU intron and is the only chloroplast-encoded maturase/splicing factor retained in most autotrophic lineages. This matches the UniProt annotation for a MatK-family intron maturase. | Comparative plastid genomics; functional studies in land-plant homologs | Conserved across autotrophic land plants with chloroplast group II introns; knockout attempts in tobacco did not yield homoplastomic mutants, consistent with essentiality. | Zoschke et al. 2010, PNAS, doi:10.1073/pnas.0909400107, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 1-1); Hertel et al. 2013, Plant Physiology, doi:10.1104/pp.113.227579, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9); Mizrahi et al. 2022, Genes, doi:10.3390/genes13071137, https://doi.org/10.3390/genes13071137 (mizrahi2022groupiiintronencoded pages 6-7) |
| Domains | MatK is a degenerated group II intron maturase/IEP that retains the maturase domain X and only part of the reverse-transcriptase region, while lacking the DNA endonuclease/mobility modules seen in canonical bacterial group II intron proteins. This supports a specialization for RNA splicing rather than intron mobility. | Domain/evolutionary inference integrated with biochemical data | Structural degeneration is consistent with loss of mobility and retention of splicing activity; direct biochemical support for maturase activity was demonstrated in vitro. | Barthet et al. 2020, Plant Direct, doi:10.1002/pld3.208, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2); Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 1-1); Qu 2015 dissertation, doi:10.18452/17256, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 18-21, qu2015analysisoftargets pages 15-18) |
| Localization | MatK is a chloroplast stromal/soluble protein rather than a membrane protein. Its activity is therefore placed in the chloroplast stroma, where plastid pre-RNAs are processed and group II introns are spliced. | Chloroplast transformation, organelle fractionation, immunoblotting | In tobacco, MatK accumulation was highest in very young tissue, peaking at day 7 post-imbibition, then declining strongly in older tissue. | Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 1-1, zoschke2010anorganellarmaturase pages 3-3); Hertel et al. 2013, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9) |
| Molecular function | Primary function: facilitation of chloroplast group IIA intron excision/splicing in precursor RNAs. MatK acts in trans on multiple introns, not just its host intron, and likely promotes correct RNA folding/assembly of catalytically competent intron structures. | RIP-Chip/RIP-seq, developmental expression analysis, in vitro splicing assay, genetic inference from plastid translation-deficient mutants | Barthet et al. showed the first direct biochemical evidence: addition of recombinant MatK increased rps12 intron 2 self-splicing efficiency in vitro, but not rpl2 under the tested conditions. | Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 3-3, zoschke2010anorganellarmaturase pages 1-1); Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2); Hertel et al. 2013, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9) |
| Validated intron targets | Seven canonical chloroplast group IIA intron targets repeatedly associated with MatK are: trnK, trnA, trnI, trnV, atpF, rpl2, and rps12 intron 2. These are the best-supported conserved targets relevant for annotation of T. arvense MatK by homology. | RNA immunoprecipitation/chip or sequencing; comparative functional inference | RIP-based studies recovered association with 7 canonical group IIA introns; all known strong targets fall in subgroup IIA. | Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 1-1); Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2); Qu 2015, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 18-21, qu2015analysisoftargets pages 56-60) |
| trnK target summary | MatK is encoded in the trnK intron and binds intronic regions flanking rather than the matK ORF itself; this supports action on its home intron while also acting on other introns in trans. | RIP-Chip mapping of binding regions | Strong enrichment mapped to intron regions upstream/downstream of the matK ORF; authors did not observe strongest enrichment over the matK coding region itself. | Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 3-3, zoschke2010anorganellarmaturase pages 1-1) |
| trnA target summary | trnA is one of the canonical group IIA introns associated with MatK and is consistently included among inferred/observed MatK targets in land plants. | RIP-chip / RIP-seq association; review synthesis | Included among the 7 principal MatK-associated introns in chloroplasts. | Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2); Qu 2015, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 18-21, qu2015analysisoftargets pages 56-60) |
| trnI target summary | trnI is a canonical MatK-associated chloroplast group IIA intron target. | RIP-chip / RIP-seq association; review synthesis | Included among the 7 principal MatK-associated introns in chloroplasts. | Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2); Qu 2015, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 18-21, qu2015analysisoftargets pages 56-60) |
| trnV target summary | trnV is a canonical MatK target; developmental RIP-qPCR suggested changing association over development. | RIP-based developmental interaction profiling | MatK association with trnV decreased ~2-fold in older (25-day) vs young (7-day) tobacco tissue. | Hertel et al. 2013, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9); Qu 2015, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 60-63) |
| atpF target summary | atpF is a canonical MatK target and a well-supported example of developmentally regulated MatK-RNA association. | RIP-qPCR / RIP-seq | MatK association with atpF increased ~3-fold in 25-day vs 7-day tobacco tissue. | Hertel et al. 2013, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9); Qu 2015, https://doi.org/10.18452/17256 (qu2015analysisoftargets pages 60-63) |
| rpl2 target summary | rpl2 is a canonical MatK target; in vitro, its intron can self-excise, but MatK addition did not increase splicing efficiency under the assay conditions tested. | In vitro self-splicing assay with recombinant MatK | Direct assay showed no enhancement for rpl2 in the reported experimental setup, unlike rps12 intron 2. | Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2) |
| rps12 intron 2 target summary | rps12 intron 2 is a canonical MatK target and currently has the clearest direct biochemical support for MatK-mediated stimulation of splicing. | In vitro splicing assay with recombinant MatK | Recombinant MatK increased self-splicing efficiency of rps12 intron 2; this was presented as the first direct evidence of MatK maturase activity. | Barthet et al. 2020, https://doi.org/10.1002/pld3.208 (barthet2020unravelingtherole pages 1-2) |
| Expression / regulation | MatK expression is developmentally regulated at multiple checkpoints; protein abundance does not track mRNA abundance, implying post-transcriptional regulation and/or altered protein stability. An autoregulatory model involving pre-trnK/MatK complexes has been proposed. | Quantitative expression profiling; mathematical modeling | Protein maximum at 7 dpi, pre-trnK-matK maximum around 25 dpi, mature trnK maximum around 59 dpi; pre-trnK/MatK complex ratio RR25d/7d = 1.24 in the model. | Hertel et al. 2013, https://doi.org/10.1104/pp.113.227579 (hertel2013multiplecheckpointsfor pages 8-9); Zoschke et al. 2010, https://doi.org/10.1073/pnas.0909400107 (zoschke2010anorganellarmaturase pages 1-1) |
| Current applications: plant DNA barcoding | Outside functional biology, matK DNA sequence is widely used as a plant barcode and phylogenetic marker. Its practical performance varies by taxon and primer design; it is often used with additional loci rather than alone. | Applied barcoding studies and review synthesis | In invasive plants (91 species), overall PCR+sequencing success across four loci was 87.9%; rbcL+matK gave 68.6% discrimination, while ITS+trnH-psbA reached 97.1%. In Cactaceae, BLAST-based matK identification reached 83.33% genus and 50% species; universal matK primers amplified <10%, but lineage-specific primers raised amplification to 91.95% and sequence recovery to 54.16%. | Nath et al. 2024, Plant Direct, doi:10.1002/pld3.615, https://doi.org/10.1002/pld3.615 (nath2024dnabarcodingof pages 9-10, nath2024dnabarcodingof pages 2-3); Wei et al. 2024, Pakistan Journal of Botany, doi:10.30848/pjb2024-5(11), https://doi.org/10.30848/pjb2024-5(11) (wei2024effectivenessofdna pages 3-4, wei2024effectivenessofdna pages 1-2, wei2024effectivenessofdna pages 11-15) |
| Current applications: forensic / multi-locus barcoding interpretation | Recent reviews conclude matK remains useful, but single-locus performance is inconsistent; multi-marker or super-barcode approaches usually improve species discrimination. | Review of applied barcoding datasets | Review-cited examples reported matK 91.8% recovery in one wood-forensics context, but only 62.5% species-identification success in a Paphiopedilum dataset; 3-marker combinations averaged 91.4%, and psbA-trnH + trnK reached 100% in one study. | Behura et al. 2024, Biosciences Biotechnology Research Asia, doi:10.13005/bbra/3275, https://doi.org/10.13005/bbra/3275 (behura2024differentdnabarcoding pages 7-9) |
Table: This table summarizes the conserved functional annotation of chloroplast MatK relevant to UniProt Q9GF35 from Thlaspi arvense, integrating core mechanistic evidence, validated intron targets, localization, regulation, and recent applied barcoding data. It is useful for distinguishing MatK’s primary biological role as a plastid intron maturase from its widespread use as a DNA barcode marker.
References
(zoschke2010anorganellarmaturase pages 1-1): Reimo Zoschke, Masayuki Nakamura, Karsten Liere, Masahiro Sugiura, Thomas Börner, and Christian Schmitz-Linneweber. An organellar maturase associates with multiple group ii introns. Proceedings of the National Academy of Sciences, 107:3245-3250, Jan 2010. URL: https://doi.org/10.1073/pnas.0909400107, doi:10.1073/pnas.0909400107. This article has 200 citations and is from a highest quality peer-reviewed journal.
(mizrahi2022groupiiintronencoded pages 6-7): Ron Mizrahi, Sofia Shevtsov-Tal, and Oren Ostersetzer-Biran. Group ii intron-encoded proteins (ieps/maturases) as key regulators of nad1 expression and complex i biogenesis in land plant mitochondria. Genes, 13:1137, Jun 2022. URL: https://doi.org/10.3390/genes13071137, doi:10.3390/genes13071137. This article has 10 citations.
(barthet2020unravelingtherole pages 1-2): Michelle M. Barthet, Christopher L. Pierpont, and Emilie‐Katherine Tavernier. Unraveling the role of the enigmatic matk maturase in chloroplast group iia intron excision. Plant Direct, Mar 2020. URL: https://doi.org/10.1002/pld3.208, doi:10.1002/pld3.208. This article has 45 citations and is from a peer-reviewed journal.
(qu2015analysisoftargets pages 18-21): Yujiao Qu. Analysis of targets and functions of the chloroplast intron maturase matk. ArXiv, Jun 2015. URL: https://doi.org/10.18452/17256, doi:10.18452/17256. This article has 0 citations.
(zoschke2010anorganellarmaturase pages 3-3): Reimo Zoschke, Masayuki Nakamura, Karsten Liere, Masahiro Sugiura, Thomas Börner, and Christian Schmitz-Linneweber. An organellar maturase associates with multiple group ii introns. Proceedings of the National Academy of Sciences, 107:3245-3250, Jan 2010. URL: https://doi.org/10.1073/pnas.0909400107, doi:10.1073/pnas.0909400107. This article has 200 citations and is from a highest quality peer-reviewed journal.
(hertel2013multiplecheckpointsfor pages 8-9): Stefanie Hertel, Reimo Zoschke, Laura Neumann, Yujiao Qu, Ilka M. Axmann, and Christian Schmitz-Linneweber. Multiple checkpoints for the expression of the chloroplast-encoded splicing factor matk. Plant Physiology, 163(4):1686-1698, Oct 2013. URL: https://doi.org/10.1104/pp.113.227579, doi:10.1104/pp.113.227579. This article has 23 citations and is from a highest quality peer-reviewed journal.
(qu2015analysisoftargets pages 60-63): Yujiao Qu. Analysis of targets and functions of the chloroplast intron maturase matk. ArXiv, Jun 2015. URL: https://doi.org/10.18452/17256, doi:10.18452/17256. This article has 0 citations.
(primandiri2024thematurasek pages 1-5): Poppy Rahmatika Primandiri, Muhammad Rifqi Hariri, Tutut Indah Sulistiyowati, and Agus Muji Santoso. The maturase k region of kebak, a javanese cultural flora. Advances in Social Science, Education and Humanities Research, pages 408-414, Jan 2024. URL: https://doi.org/10.2991/978-2-38476-283-5_38, doi:10.2991/978-2-38476-283-5_38. This article has 0 citations.
(nath2024dnabarcodingof pages 2-3): Sneha Nath, Joshua T. VanSlambrouck, Janelle W. Yao, Ashika Gullapalli, Fayyaz Razi, and Yan Lu. Dna barcoding of terrestrial invasive plant species in southwest michigan. Plant Direct, Jun 2024. URL: https://doi.org/10.1002/pld3.615, doi:10.1002/pld3.615. This article has 10 citations and is from a peer-reviewed journal.
(nath2024dnabarcodingof pages 9-10): Sneha Nath, Joshua T. VanSlambrouck, Janelle W. Yao, Ashika Gullapalli, Fayyaz Razi, and Yan Lu. Dna barcoding of terrestrial invasive plant species in southwest michigan. Plant Direct, Jun 2024. URL: https://doi.org/10.1002/pld3.615, doi:10.1002/pld3.615. This article has 10 citations and is from a peer-reviewed journal.
(wei2024effectivenessofdna pages 3-4): Lihua Wei, Flor Cristina Pacheco-Reyes, José Ángel Villarreal-Quintanilla, Valentín Robledo-Torres, Juan Antonio Encina-Domínguez, Edgar Eduardo Lara-Ramírez, and Miguel Ángel Pérez-Rodríguez. Effectiveness of dna barcodes (rbcl, matk, its2) in identifying genera and species in cactaceae. Pakistan Journal of Botany, Mar 2024. URL: https://doi.org/10.30848/pjb2024-5(11), doi:10.30848/pjb2024-5(11). This article has 10 citations and is from a peer-reviewed journal.
(wei2024effectivenessofdna pages 1-2): Lihua Wei, Flor Cristina Pacheco-Reyes, José Ángel Villarreal-Quintanilla, Valentín Robledo-Torres, Juan Antonio Encina-Domínguez, Edgar Eduardo Lara-Ramírez, and Miguel Ángel Pérez-Rodríguez. Effectiveness of dna barcodes (rbcl, matk, its2) in identifying genera and species in cactaceae. Pakistan Journal of Botany, Mar 2024. URL: https://doi.org/10.30848/pjb2024-5(11), doi:10.30848/pjb2024-5(11). This article has 10 citations and is from a peer-reviewed journal.
(behura2024differentdnabarcoding pages 7-9): Nisruti Anuja Behura, Naga Jogayya Kothakota, Sheerin Bashar, and Pravallika Vataparthi. Different dna barcoding techniques in forensic botany: a review. Biosciences Biotechnology Research Asia, 21:935-945, Sep 2024. URL: https://doi.org/10.13005/bbra/3275, doi:10.13005/bbra/3275. This article has 3 citations.
(qu2015analysisoftargets pages 15-18): Yujiao Qu. Analysis of targets and functions of the chloroplast intron maturase matk. ArXiv, Jun 2015. URL: https://doi.org/10.18452/17256, doi:10.18452/17256. This article has 0 citations.
(qu2015analysisoftargets pages 56-60): Yujiao Qu. Analysis of targets and functions of the chloroplast intron maturase matk. ArXiv, Jun 2015. URL: https://doi.org/10.18452/17256, doi:10.18452/17256. This article has 0 citations.
(wei2024effectivenessofdna pages 11-15): Lihua Wei, Flor Cristina Pacheco-Reyes, José Ángel Villarreal-Quintanilla, Valentín Robledo-Torres, Juan Antonio Encina-Domínguez, Edgar Eduardo Lara-Ramírez, and Miguel Ángel Pérez-Rodríguez. Effectiveness of dna barcodes (rbcl, matk, its2) in identifying genera and species in cactaceae. Pakistan Journal of Botany, Mar 2024. URL: https://doi.org/10.30848/pjb2024-5(11), doi:10.30848/pjb2024-5(11). This article has 10 citations and is from a peer-reviewed journal.