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Article: Structural basis of DNA replication origin recognition by human Orc6 protein binding with DNA

TitleStructural basis of DNA replication origin recognition by human Orc6 protein binding with DNA
Authors
Issue Date2020
PublisherOxford University Press: Policy C - Creative Commons Attribution and Creative Commons Attribution Non-Commercial. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2020, v. 48, p. 11146-11161 How to Cite?
AbstractThe six-subunit origin recognition complex (ORC), a DNA replication initiator, defines the localization of the origins of replication in eukaryotes. The Orc6 subunit is the smallest and the least conserved among ORC subunits. It is required for DNA replication and essential for viability in all species. Orc6 in metazoans carries a structural homology with transcription factor TFIIB and can bind DNA on its own. Here, we report a solution structure of the full-length human Orc6 (HsOrc6) alone and in a complex with DNA. We further showed that human Orc6 is composed of three independent domains: N-terminal, middle and C-terminal (HsOrc6-N, HsOrc6-M and HsOrc6-C). We also identified a distinct DNA-binding domain of human Orc6, named as HsOrc6-DBD. The detailed analysis of the structure revealed novel amino acid clusters important for the interaction with DNA. Alterations of these amino acids abolish DNA-binding ability of Orc6 and result in reduced levels of DNA replication. We propose that Orc6 is a DNA-binding subunit of human/metazoan ORC and may play roles in targeting, positioning and assembling the functional ORC at the origins.
Persistent Identifierhttp://hdl.handle.net/10722/295772
ISSN
2023 Impact Factor: 16.6
2023 SCImago Journal Rankings: 7.048
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorXu, N-
dc.contributor.authorYou, Y-
dc.contributor.authorLiu, C-
dc.contributor.authorBalasov, M-
dc.contributor.authorLun, LT-
dc.contributor.authorGeng, Y-
dc.contributor.authorFung, CP-
dc.contributor.authorMiao, H-
dc.contributor.authorTian, H-
dc.contributor.authorChoy, TT-
dc.contributor.authorShi, X-
dc.contributor.authorFan, Z-
dc.contributor.authorZhou, B-
dc.contributor.authorAkhmetova, K-
dc.contributor.authorDin, RU-
dc.contributor.authorYang, H-
dc.contributor.authorHao, Q-
dc.contributor.authorQian, P-
dc.contributor.authorChesnokov, I-
dc.contributor.authorZhu, G-
dc.date.accessioned2021-02-08T08:13:47Z-
dc.date.available2021-02-08T08:13:47Z-
dc.date.issued2020-
dc.identifier.citationNucleic Acids Research, 2020, v. 48, p. 11146-11161-
dc.identifier.issn0305-1048-
dc.identifier.urihttp://hdl.handle.net/10722/295772-
dc.description.abstractThe six-subunit origin recognition complex (ORC), a DNA replication initiator, defines the localization of the origins of replication in eukaryotes. The Orc6 subunit is the smallest and the least conserved among ORC subunits. It is required for DNA replication and essential for viability in all species. Orc6 in metazoans carries a structural homology with transcription factor TFIIB and can bind DNA on its own. Here, we report a solution structure of the full-length human Orc6 (HsOrc6) alone and in a complex with DNA. We further showed that human Orc6 is composed of three independent domains: N-terminal, middle and C-terminal (HsOrc6-N, HsOrc6-M and HsOrc6-C). We also identified a distinct DNA-binding domain of human Orc6, named as HsOrc6-DBD. The detailed analysis of the structure revealed novel amino acid clusters important for the interaction with DNA. Alterations of these amino acids abolish DNA-binding ability of Orc6 and result in reduced levels of DNA replication. We propose that Orc6 is a DNA-binding subunit of human/metazoan ORC and may play roles in targeting, positioning and assembling the functional ORC at the origins.-
dc.languageeng-
dc.publisherOxford University Press: Policy C - Creative Commons Attribution and Creative Commons Attribution Non-Commercial. The Journal's web site is located at http://nar.oxfordjournals.org/-
dc.relation.ispartofNucleic Acids Research-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleStructural basis of DNA replication origin recognition by human Orc6 protein binding with DNA-
dc.typeArticle-
dc.identifier.emailHao, Q: qhao@hku.hk-
dc.identifier.authorityHao, Q=rp01332-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1093/nar/gkaa751-
dc.identifier.pmid32986843-
dc.identifier.pmcidPMC7641730-
dc.identifier.scopuseid_2-s2.0-85095799247-
dc.identifier.hkuros321224-
dc.identifier.volume48-
dc.identifier.spage11146-
dc.identifier.epage11161-
dc.identifier.isiWOS:000606018400043-
dc.publisher.placeUnited Kingdom-

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