Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing.
Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex.
Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase.
Architecture of the yeast origin recognition complex bound to origins of DNA replication.
Formation of a preinitiation complex by S-phase cyclin CDK-dependent loading of Cdc45p onto chromatin.
Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae.
Differential DNA affinity specifies roles for the origin recognition complex in budding yeast heterochromatin.
Proteome survey reveals modularity of the yeast cell machinery.
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Structure and function of the Saccharomyces cerevisiae Sir3 BAH domain.
Cell cycle execution point analysis of ORC function and characterization of the checkpoint response to ORC inactivation in Saccharomyces cerevisiae.
Reconstitution of Saccharomyces cerevisiae prereplicative complex assembly in vitro.
Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.
Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.
The architecture of the DNA replication origin recognition complex in Saccharomyces cerevisiae.
Defining the budding yeast chromatin-associated interactome.
Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy.
An inter-species protein-protein interaction network across vast evolutionary distance.
Structure and function of the Orc1 BAH-nucleosome complex.
Establishment and function of chromatin organization at replication origins.
The social and structural architecture of the yeast protein interactome.
CDT1-mediated loading of MCM2-7 to replication origin in budding yeast
ATP-dependent release of CDT1 from the OCCM complex in budding yeast
CTD1-mediated formation of MCM2-7 double hexamers at the replication origins in budding yeast
Falcon deep research report on ORC1 (yeast)
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Orc1 (YML065W; UniProt P54784) is the largest, ~914-aa subunit of the heterohexameric
origin recognition complex (ORC, Orc1-6), with an N-terminal BAH domain and a
C-terminal AAA+ ATPase region.
"encodes **Origin Recognition Complex subunit 1 (Orc1)**, a ~914-aa protein that is part of the heterohexameric ORC (Orc1–6)"
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Orc1 has two separable functional modules: an AAA+ initiator module for ATP-dependent
origin recognition/licensing, and an N-terminal BAH chromatin-binding module that
mediates nucleosome binding and recruitment to silencing-associated chromatin.
"an **AAA+ initiator module** contributing to ATP-dependent origin recognition/licensing, and an N-terminal **BAH chromatin-binding module** that mediates nucleosome binding and recruitment to silencing-associated chromatin sites"
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Orc1 is the only ORC subunit experimentally demonstrated to have ATPase activity,
and ATP binding by Orc1 is required for ORC DNA binding, while ATP hydrolysis is
not always required for the binding step itself.
"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"
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ORC binds sequence-defined ARS elements and, with Cdc6 and Cdt1, loads MCM2-7 to
form the pre-replicative complex; in early G1 ORC recruits Cdc6 then Cdt1-MCM2-7,
loading MCM one hexamer at a time into a head-to-head double hexamer.
"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"
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The Orc1 BAH-nucleosome complex was solved at 3.3 Angstrom, with BAH making
extensive contacts to core histones and burying ~1590 square Angstrom of surface;
unlike Sir3, Orc1 BAH does not strongly discriminate H4K16 acetylation state.
"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"
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At HM silencers, the Orc1 BAH domain binds silencer elements and recruits Sir1,
which helps recruit the Sir2/Sir3/Sir4 silencing machinery to nucleate
heterochromatin.
"Orc1 BAH binds at DNA silencer elements and recruits **Sir1**, which then helps recruit the Sir2/Sir3/Sir4 silencing machinery"
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Orc1's origin-binding and silencing-locus-binding determinants are genetically
separable: deletion of the BAH domain abolishes binding at silencing-associated
sites but Orc1 remains bound to replication origins.
"Orc1 lacking the BAH domain is **lost from silencing-associated sites but remains bound to replication origins**"
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Orc1 BAH-nucleosome interactions protect rDNA border integrity during meiosis;
reduced Orc1-BAH affinity is associated with increased double-strand breaks.
"Orc1 BAH–nucleosome interactions contribute to genome stability at rDNA borders during meiosis; reduced Orc1-BAH affinity is associated with increased double-strand breaks"
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Licensing (MCM loading) is restricted to early G1; after G1, CDK-dependent
phosphorylation inhibits re-licensing to prevent rereplication.
"the **licensing reaction (MCM loading)** is concentrated in **early G1**; after G1, **CDK-dependent phosphorylation** inhibits re-licensing to prevent rereplication"
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Budding yeast uses sequence-specific ORC recognition at ARS elements, whereas
human ORC is more strongly guided by chromatin landscape, so lineage-specific
features (e.g. the Orc4 insertion helix) should not be naively extrapolated.
"yeast uses sequence-specific ORC recognition at ARSs, whereas human ORC is more strongly guided by chromatin landscape"