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.
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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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We are interested in where in or outside the cell the gene product carries out its function.
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The literature synthesized here matches the UniProt-provided identity: S. cerevisiae ORC1 (YML065W; UniProt P54784) encodes Origin Recognition Complex subunit 1 (Orc1), a ~914-aa protein that is part of the heterohexameric ORC (Orc1–6) and contains an N-terminal BAH (bromo-adjacent homology) domain and a C-terminal AAA+ ATPase region with a winged-helix domain (WHD) consistent with ORC1-family initiators. This domain architecture and function are repeatedly stated or implied across structural, genome-wide mapping, and mechanistic licensing studies (ioannes2019structureandfunction pages 1-2, chappleboim2024orderedanddisordered pages 1-1, chacin2023establishmentandfunction pages 19-22).
In eukaryotes, replication origins are “licensed” in G1 by assembling a pre-replicative complex (pre-RC), whose central event is loading the MCM2–7 helicase onto double-stranded DNA as a head-to-head double hexamer (MCM-DH). In budding yeast, ORC binds sequence-defined ARS elements and, together with Cdc6 and Cdt1, loads MCM2–7 to form the pre-RC (tye2023theoriginrecognition pages 1-2). ORC is a large (~400 kDa) heterohexamer (Orc1–6) that recognizes a replication-origin DNA consensus (ARS consensus sequence, ACS) and acts as the platform that seeds helicase loading and replication initiation (parker2017mechanismsandregulation pages 4-6, tye2023theoriginrecognition pages 2-4).
Budding-yeast replication origins (ARSs) contain a characteristic ~17 bp ARS consensus sequence (ACS); the essential core is often described as an ~11 bp motif (WTTTATRTTTW) (tye2023theoriginrecognition pages 2-4). In a recent review, >400 ARSs are noted genome-wide, with 249 described as having canonical features (tye2023theoriginrecognition pages 2-4).
A key concept for functional annotation is that Orc1 has separable modules: (i) an AAA+ initiator module contributing to ATP-dependent origin recognition/licensing, and (ii) an N-terminal BAH chromatin-binding module that mediates nucleosome binding and recruitment to silencing-associated chromatin sites (chappleboim2024orderedanddisordered pages 5-5, ioannes2019structureandfunction pages 1-2).
Orc1 is part of the AAA+ ATPase-containing ORC core; mechanistic reviews summarize that Orc1 is the only ORC subunit experimentally demonstrated to have ATPase activity, and that canonical AAA+ features (Walker A/B, arginine finger, composite active sites) help coordinate ATP binding/hydrolysis within initiator assemblies (parker2017mechanismsandregulation pages 4-6). Functional evidence further indicates that ATP binding by Orc1 is required for ORC DNA binding, while ATP hydrolysis is not always required for the binding step itself (geissenhoner2004theroleof pages 25-28). Together, these support a model where Orc1’s ATP-bound state is critical for stable, specific ORC–origin association and for engaging the co-loader Cdc6 during licensing (geissenhoner2004theroleof pages 25-28, parker2017mechanismsandregulation pages 4-6).
High-resolution cryo-EM structures of the ORC·DNA·Cdc6 intermediate provide direct mechanistic detail about ATPase-site configuration: the Orc1·Orc4 ATPase site and Cdc6·Orc1 composite site can adopt inactive/pre-hydrolysis configurations that require additional activation for catalysis, consistent with a regulated ATPase cycle during helicase recruitment/loading (schmidt2022amechanismof pages 1-2).
Budding yeast ORC recognizes origins largely via sequence-defined elements. A 2023 review reports that yeast ORC bound to 72 bp of ARS305 DNA (ACS + B1) was solved at 3.0 Å by cryo-EM, with Orc1–5 encircling DNA; Orc6 is positioned away from the main DNA-encircling module (tye2023theoriginrecognition pages 2-4). The same review describes base-specific and non-specific components of DNA recognition: Orc1 and Orc2 contribute minor-groove interactions (e.g., Orc1 basic patch), while the Orc4 insertion helix (IH) inserts into the major groove and underlies much of the sequence specificity in budding yeast (tye2023theoriginrecognition pages 2-4).
A major 2024 advance is the genome-scale dissection of ORC DNA-binding determinants by mapping 38 designed ORC mutants. This work shows that origin binding can depend on distinct Orc1 disordered basic patches and on Orc4 IH, and that origins can be partitioned into two dominant motif variants with different binding requirements (chappleboim2024orderedanddisordered pages 1-1). Specifically, replication origins contain a 17 bp motif, and origin binding in vivo can require Orc1-BP4 and Orc4-IH for one motif class, while another class can use Orc1-BP3 in place of Orc4-IH (chappleboim2024orderedanddisordered pages 1-1).
In early G1, ORC (including Orc1) recruits Cdc6, then Cdt1–MCM2–7, loading MCM one hexamer at a time to form a head-to-head MCM double hexamer (tye2023theoriginrecognition pages 1-2). Structural and mechanistic work indicates that ORC bends DNA at origin elements in a manner that helps align and insert DNA into the MCM ring during formation of helicase-loading intermediates (tye2023theoriginrecognition pages 2-4, schmidt2022amechanismof pages 1-2). The ORC·DNA·Cdc6 ring architecture and its regulation by conformational switches (including an autoinhibited state involving Orc6) are described by cryo-EM structures at ~2.5–2.7 Å resolution (schmidt2022amechanismof pages 1-2).
A central experimentally supported non-enzymatic function of Orc1 is nucleosome binding through the BAH domain. A structural study determined the Orc1 BAH–nucleosome complex at 3.3 Å and reported that Orc1 BAH forms extensive contacts with core histones, burying ~1590 Ų of surface (ioannes2019structureandfunction pages 1-2). Importantly, Orc1 differs from its paralog Sir3 in that Orc1 BAH does not strongly discriminate between acetylated and non-acetylated H4K16, consistent with a chromatin-binding role across eu- and heterochromatin (ioannes2019structureandfunction pages 1-2). Sequence similarity between Orc1 and Sir3 BAH domains is reported as 48% identity / 67% similarity (ioannes2019structureandfunction pages 1-2).
Recent genome-wide functional mapping provides in vivo support for the modularity of Orc1 targeting: Orc1 lacking the BAH domain is lost from silencing-associated sites but remains bound to replication origins, whereas an isolated Orc1 N-terminal tail (~375 aa; containing BAH) is sufficient for strong binding at silencing-associated sites (chappleboim2024orderedanddisordered pages 5-5). A peer-reviewed 2024 study further states that at silencing-associated loci lacking the canonical origin motif, ORC binding and activity are “fully explained” by the BAH domain (chappleboim2024orderedanddisordered pages 1-1).
At the silent mating-type loci, Orc1’s BAH domain plays a mechanistic role in nucleating silenced chromatin. Orc1 BAH binds at DNA silencer elements and recruits Sir1, which then helps recruit the Sir2/Sir3/Sir4 silencing machinery (ioannes2019structureandfunction pages 1-2). Structure-guided mutagenesis in a classic EMBO Journal study identified a specific helical insertion within the Orc1 BAH domain that confers Sir1-binding specificity; mutants disrupting this region phenocopied sir1Δ, producing strong defects in silencing readouts (colony color and mating-pheromone “shmooing”) with quantitative changes (e.g., ~80% resistance to α-factor and ~14–20% shmooing versus >90% shmooing in controls) (zhang2002structureandfunction pages 2-3).
ORC’s role in silencing extends beyond a single silencer-bound nucleation site. ChIP-based evidence indicates ORC can associate throughout the internal regions of HMR, including sequences lacking canonical ACS, and that this association depends on Sir proteins and silent chromatin context (ozaydın2010expandedrolesof pages 1-2). Orc1’s BAH domain and Orc1–Sir1 interaction are proposed contributors to this broader association and to silent chromatin architecture (ozaydın2010expandedrolesof pages 12-13, ozaydın2010expandedrolesof pages 1-2). Telomeric silencing is reported to depend on Orc1’s BAH domain and on N-terminal acetylation of Orc1 by NatA-Ard, linking a post-translational modification to silencing function (ioannes2019structureandfunction pages 1-2).
In addition to replication and silencing, Orc1 BAH–nucleosome interactions contribute to genome stability at rDNA borders during meiosis; reduced Orc1-BAH affinity is associated with increased double-strand breaks, implying that direct nucleosome binding is required for this protective function (ioannes2019structureandfunction pages 1-2). In one source, the rDNA locus is described as a tandem array of ~100–200 copies of a 9.1 kb repeat, with ~20% active origins (geissenhoner2004theroleof pages 25-28).
Multiple lines of evidence support that ORC is a chromatin-bound initiator that can remain associated with origin DNA across the cell cycle. One source states ORC binds ACS sites distributed genome-wide and “remains bound throughout the cell cycle,” with Orc1 ATP binding required for DNA binding (geissenhoner2004theroleof pages 25-28). Functionally, the licensing reaction (MCM loading) is concentrated in early G1; after G1, CDK-dependent phosphorylation inhibits re-licensing to prevent rereplication (tye2023theoriginrecognition pages 1-2).
Recent work emphasizes that regulation of licensing involves intrinsically disordered regulatory elements within ORC subunits (including but not limited to Orc1). A 2024 Nature Communications study identifies an Orc2 N-terminal IDR segment (residues 176–200) whose mutation impairs ATP hydrolysis in later helicase-loading transitions and blocks formation of downstream intermediates (wu2024replicationlicensingregulated pages 1-2). A 2024 preprint proposes that CDK phosphorylation of an Orc2 IDR blocks formation of a key MCM–ORC intermediate required for second-hexamer loading, shaping origin architecture and explaining how certain origins can partially escape CDK inhibition (lim2024cellcycleregulation pages 1-2).
A prominent 2023 theme is the integration of high-resolution cryo-EM structures with genetic and biochemical reconstitution, enabling explicit structural hypotheses about origin selection and helicase loading (tye2023theoriginrecognition pages 2-4, tye2023theoriginrecognition pages 1-2). In 2024, this structural understanding is complemented by genome-wide mutant binding maps demonstrating that ORC’s DNA-binding logic is modular and context-dependent: disordered Orc1 basic patches contribute to motif-specific origin binding, while Orc1 BAH explains binding at non-origin silencing-associated loci (chappleboim2024orderedanddisordered pages 1-1).
A clear recent advance is the experimental separation of Orc1’s origin-binding determinants from its silencing-locus determinants. In vivo, loss of BAH abolishes binding at silencing-associated loci but not at origins, while origin binding can be strongly reduced by deletion of Orc1-BP4 (which is also reported essential for growth) (chappleboim2024orderedanddisordered pages 5-5). This supports the modern view that ORC uses different interfaces for “replication origin” versus “silent chromatin” genomic occupancy (chappleboim2024orderedanddisordered pages 5-5, chappleboim2024orderedanddisordered pages 1-1).
A recent review explicitly contrasts yeast and human origin selection strategies: yeast uses sequence-specific ORC recognition at ARSs, whereas human ORC is more strongly guided by chromatin landscape, and pre-RCs can form distant from ORC binding sites (tye2023theoriginrecognition pages 1-2). This comparative framing supports an expert consensus that budding yeast ORC (and Orc1) remains the clearest mechanistic paradigm for origin licensing because origin sequences are compact and experimentally tractable, while also highlighting which features (e.g., Orc4 insertion helix) are lineage-specific and thus should not be naively extrapolated (tye2023theoriginrecognition pages 2-4, tye2023theoriginrecognition pages 1-2).
Orc1 (ORC1/YML065W; UniProt P54784) is a chromatin-associated initiator protein and the largest subunit of ORC that (i) supports ATP-dependent, sequence-specific origin recognition and pre-RC assembly through AAA+ initiator mechanisms, DNA bending, and regulated ATPase-site configurations that coordinate recruitment/loading of Cdc6 and MCM2–7 (tye2023theoriginrecognition pages 2-4, schmidt2022amechanismof pages 1-2, parker2017mechanismsandregulation pages 4-6), and (ii) mediates chromatin/nucleosome interactions and transcriptional silencing via its N-terminal BAH domain, which binds nucleosomes, recruits Sir1 at HM silencers, contributes to telomeric silencing (including via NatA-mediated acetylation), and supports rDNA border integrity during meiosis (ioannes2019structureandfunction pages 1-2, zhang2002structureandfunction pages 2-3, chappleboim2024orderedanddisordered pages 5-5).
Within the retrieved evidence set, Orc1’s ATPase function is described qualitatively and structurally, but explicit kinetic parameters (e.g., kcat/Km for Orc1 ATP hydrolysis) were not captured in the available excerpts; answering that precisely would require targeted retrieval of dedicated biochemical enzymology papers beyond the current set (parker2017mechanismsandregulation pages 4-6, schmidt2022amechanismof pages 1-2).
| Functional aspect | Key mechanistic details | Quantitative/data points | Key recent sources (date; URL) |
|---|---|---|---|
| Origin licensing | Orc1 is the largest ORC subunit in the six-subunit origin recognition complex that binds budding-yeast replication origins in an ATP-dependent manner. In early G1, ORC with Cdc6 recruits Cdt1-Mcm2-7 and loads a head-to-head MCM double hexamer to form the pre-replicative complex; cryo-EM work shows ORC bends origin DNA and positions it for helicase loading. Orc1 contributes DNA-contacting/basic elements within the ORC-DNA interface and participates in the ATPase architecture that coordinates loading. (tye2023theoriginrecognition pages 1-2, schmidt2022amechanismof pages 1-2, tye2023theoriginrecognition pages 2-4) | ARS consensus sequence (ACS) is 17 bp; essential core often described as 11 bp (WTTTATRTTTW). >400 ARSs identified genome-wide, with 249 canonical features noted in the review. Yeast ORC bound to 72 bp of ARS305 (ACS+B1) solved at 3.0 Å; ORC-Cdc6-DNA intermediates reported at ~2.5-2.7 Å. (tye2023theoriginrecognition pages 1-2, tye2023theoriginrecognition pages 2-4, schmidt2022amechanismof pages 1-2) | Tye & Zhai, 2023, Biology (Dec 2023): https://doi.org/10.3390/biology13010013 ; Feng et al., 2021, Nat Commun (Jun 2021): https://doi.org/10.1038/s41467-021-24199-1 ; Schmidt et al., 2022, Nat Commun (Feb 2022): https://doi.org/10.1038/s41467-022-28695-w |
| ATPase / DNA binding | Orc1 belongs to the AAA+ ATPase-containing ORC core; reviews identify Orc1 as the only ORC subunit experimentally demonstrated to have ATPase activity. The Orc1-Orc4 and Cdc6-Orc1 composite ATPase sites are central to origin licensing, and ATP binding is required for origin-specific DNA binding and MCM loading. DNA recognition combines base-specific and backbone contacts: Orc1 basic patches engage the DNA minor groove, while Orc4 insertion helix contacts the major groove. Genome-wide mutagenesis shows different Orc1 basic patches contribute differentially across origin classes. (parker2017mechanismsandregulation pages 4-6, schmidt2022amechanismof pages 1-2, chappleboim2024orderedanddisordered pages 1-1, tye2023theoriginrecognition pages 2-4) | ORC is ~400 kDa. Cryo-EM structural work used truncated Orc1 residues 355-914 for some ORC-DNA analyses. Orc1-BP4 modeled at aa 356-373; MD used a 20-nt ARS segment. Genome-wide study tested 38 designed ORC mutants and analyzed top 150 bound origins within 300-bp windows. (parker2017mechanismsandregulation pages 4-6, chappleboim2024orderedanddisordered pages 1-1, chappleboim2024orderedanddisordered pages 3-4) | Chappleboim et al., 2024, Nucleic Acids Res (Apr 2024): https://doi.org/10.1093/nar/gkae249 ; Tye & Zhai, 2023, Biology (Dec 2023): https://doi.org/10.3390/biology13010013 ; Parker et al., 2017, Crit Rev Biochem Mol Biol (Jan 2017): https://doi.org/10.1080/10409238.2016.1274717 |
| Chromatin / BAH nucleosome binding | The N-terminal BAH domain of Orc1 is a chromatin-binding module distinct from the AAA+ region. Structural work shows Orc1 BAH binds the nucleosome core directly, contacting histones H2A/H2B/H3/H4 and helping target ORC to a class of origins and chromatin sites. Unlike Sir3, Orc1 BAH does not strongly discriminate H4K16 acetylation state, consistent with function in both eu- and heterochromatin. Recent genome-wide work shows BAH is dispensable for binding at canonical origins but essential for binding/activity at silencing-associated loci lacking the canonical motif. (ioannes2019structureandfunction pages 1-2, chappleboim2024orderedanddisordereda pages 3-5, chappleboim2024orderedanddisordered pages 12-12, tye2023theoriginrecognition pages 6-8) | Orc1 is 914 aa. Orc1 BAH-nucleosome structure solved at 3.3 Šand buries ~1590 Ų of surface. Orc1/Sir3 BAH similarity reported as 48% identity and 67% similarity. An isolated ~375-aa Orc1 N-terminal tail containing BAH retained strong binding to silencing-associated loci. (ioannes2019structureandfunction pages 1-2, chappleboim2024orderedanddisordereda pages 3-5, chacin2023establishmentandfunction pages 19-22) | Chappleboim et al., 2024, Nucleic Acids Res (Apr 2024): https://doi.org/10.1093/nar/gkae249 ; De Ioannes et al., 2019, Nat Commun (Jul 2019): https://doi.org/10.1038/s41467-019-10609-y ; Tye & Zhai, 2023, Biology (Dec 2023): https://doi.org/10.3390/biology13010013 |
| Silencing / heterochromatin | Beyond replication, Orc1 has a well-established silencing role through its BAH domain. At HM silencers, Orc1 BAH helps recruit Sir1 and nucleate SIR-mediated heterochromatin. Structural/functional studies also support Orc1 roles at telomeres and in protecting rDNA borders during meiosis through direct chromatin interactions. Recent in vivo mapping indicates silencing-associated ORC sites lacking the replication motif are explained largely by BAH-mediated targeting. (ioannes2019structureandfunction pages 1-2, chappleboim2024orderedanddisordereda pages 3-5, chappleboim2024orderedanddisordered pages 12-12) | HM silencing-associated sites can retain Orc1 N-tail/BAH binding even when canonical origin-like recognition is absent. rDNA arrays are reported as ~100-200 copies of a 9.1 kb repeat, with only ~20% of repeats functioning as active origins in one cited source. (chappleboim2024orderedanddisordereda pages 3-5, geissenhoner2004theroleof pages 25-28) | Dhillon & Kamakaka, 2024, Epigenetics & Chromatin (Sep 2024): https://doi.org/10.1186/s13072-024-00553-7 ; De Ioannes et al., 2019, Nat Commun (Jul 2019): https://doi.org/10.1038/s41467-019-10609-y ; Hou et al., 2005, PNAS (Jun 2005): https://doi.org/10.1073/pnas.0503525102 ; Zhang et al., 2002, EMBO J (Sep 2002): https://doi.org/10.1093/emboj/cdf468 |
| Regulation | ORC activity is cell-cycle regulated to permit licensing only in G1. CDK-dependent phosphorylation inhibits re-licensing after G1. Recent work highlights regulatory intrinsically disordered regions (IDRs): Orc2 contains a short linear motif/IDR segment needed for MO intermediate formation and second-hexamer loading, and CDK phosphorylation of this IDR blocks MO and double-hexamer assembly. Separate structural work identified an autoinhibitory ORC-Cdc6-DNA state in which Orc6 blocks productive MCM docking. These studies place Orc1 within a broader ORC regulatory network controlling helicase loading and preventing rereplication. (tye2023theoriginrecognition pages 1-2, lim2024cellcycleregulation pages 1-2, wu2024replicationlicensingregulated pages 1-2, schmidt2022amechanismof pages 1-2) | Orc2 IDR segment 176-200, with key residue I194, is essential; Orc2 CDK phosphosites include S206, T217, T219. Origins with two high-affinity ORC sites can bypass the MO-dependent pathway and partially escape CDK inhibition. Orc4 insertion helix is a 19-aa insertion; deleting it yields viable cells with prolonged G2 and Rad53 phosphorylation. (lim2024cellcycleregulation pages 1-2, wu2024replicationlicensingregulated pages 1-2, tye2023theoriginrecognition pages 2-4) | Wu et al., 2024, Nat Commun (Sep 2024): https://doi.org/10.1038/s41467-024-52408-0 ; Lim et al., 2024, bioRxiv (Jan 2024): https://doi.org/10.1101/2024.01.10.575016 ; Schmidt et al., 2022, Nat Commun (Feb 2022): https://doi.org/10.1038/s41467-022-28695-w ; Tye & Zhai, 2023, Biology (Dec 2023): https://doi.org/10.3390/biology13010013 |
Table: This table summarizes the main experimentally supported functions of Saccharomyces cerevisiae Orc1, separating its replication-initiation, ATPase/DNA-binding, chromatin-binding, silencing, and regulatory roles. It emphasizes recent 2023-2024 studies while retaining seminal mechanistic papers for context.
References
(ioannes2019structureandfunction pages 1-2): Pablo De Ioannes, Victor A. Leon, Zheng Kuang, Miao Wang, Jef D. Boeke, Andreas Hochwagen, and Karim-Jean Armache. Structure and function of the orc1 bah-nucleosome complex. Nature Communications, Jul 2019. URL: https://doi.org/10.1038/s41467-019-10609-y, doi:10.1038/s41467-019-10609-y. This article has 52 citations and is from a highest quality peer-reviewed journal.
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(chacin2023establishmentandfunction pages 19-22): Erika Chacin. Establishment and function of nucleosome organization at eukaryotic chromosome replication origins. Dissertation, Jan 2023. URL: https://doi.org/10.5282/edoc.33330, doi:10.5282/edoc.33330. This article has 0 citations.
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(zhang2002structureandfunction pages 2-3): Zhiguo Zhang, M. Hayashi, O. Merkel, B. Stillman, and R. Xu. Structure and function of the bah‐containing domain of orc1p in epigenetic silencing. The EMBO Journal, 21:4600-4611, Sep 2002. URL: https://doi.org/10.1093/emboj/cdf468, doi:10.1093/emboj/cdf468. This article has 143 citations.
(ozaydın2010expandedrolesof pages 1-2): Bilge Özaydın and Jasper Rine. Expanded roles of the origin recognition complex in the architecture and function of silenced chromatin in saccharomyces cerevisiae. Feb 2010. URL: https://doi.org/10.1128/mcb.00614-09, doi:10.1128/mcb.00614-09. This article has 29 citations and is from a domain leading peer-reviewed journal.
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(wu2024replicationlicensingregulated pages 1-2): Yue Wu, Qiongdan Zhang, Yuhan Lin, Wai Hei Lam, and Yuanliang Zhai. Replication licensing regulated by a short linear motif within an intrinsically disordered region of origin recognition complex. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52408-0, doi:10.1038/s41467-024-52408-0. This article has 5 citations and is from a highest quality peer-reviewed journal.
(lim2024cellcycleregulation pages 1-2): Chew Theng Lim, Thomas C.R. Miller, Kang Wei Tan, Saurabh Talele, Anne Early, Philip East, Humberto Sánchez, Nynke H. Dekker, Alessandro Costa, and John F.X. Diffley. Cell cycle regulation has shaped budding yeast replication origin structure and function. bioRxiv, Jan 2024. URL: https://doi.org/10.1101/2024.01.10.575016, doi:10.1101/2024.01.10.575016. This article has 9 citations.
(chappleboim2024orderedanddisordered pages 3-4): Michal Chappleboim, Segev Naveh-Tassa, Miri Carmi, Yaakov Levy, and Naama Barkai. Ordered and disordered regions of the origin recognition complex direct differential in vivo binding at distinct motif sequences. Nucleic Acids Research, 52:5720-5731, Apr 2024. URL: https://doi.org/10.1093/nar/gkae249, doi:10.1093/nar/gkae249. This article has 7 citations and is from a highest quality peer-reviewed journal.
(chappleboim2024orderedanddisordereda pages 3-5): Michal Chappleboim, Segev Naveh-Tassa, Miri Carmi, Yaakov Levy, and Naama Barkai. Ordered and disordered regions of the origin recognition complex (orc) combine to direct in-vivo binding at symmetric and non-symmetric motif sequences. bioRxiv, Jan 2024. URL: https://doi.org/10.1101/2024.01.27.577596, doi:10.1101/2024.01.27.577596. This article has 0 citations.
(chappleboim2024orderedanddisordered pages 12-12): Michal Chappleboim, Segev Naveh-Tassa, Miri Carmi, Yaakov Levy, and Naama Barkai. Ordered and disordered regions of the origin recognition complex direct differential in vivo binding at distinct motif sequences. Nucleic Acids Research, 52:5720-5731, Apr 2024. URL: https://doi.org/10.1093/nar/gkae249, doi:10.1093/nar/gkae249. This article has 7 citations and is from a highest quality peer-reviewed journal.
(tye2023theoriginrecognition pages 6-8): Bik-Kwoon Tye and Yuanliang Zhai. The origin recognition complex: from origin selection to replication licensing in yeast and humans. Biology, 13:13, Dec 2023. URL: https://doi.org/10.3390/biology13010013, doi:10.3390/biology13010013. This article has 10 citations.