File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1038/s41586-018-0293-x
- Scopus: eid_2-s2.0-85049837013
- WOS: WOS:000438240900048
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Structure of the origin recognition complex bound to DNA replication origin
Title | Structure of the origin recognition complex bound to DNA replication origin |
---|---|
Authors | |
Issue Date | 2018 |
Citation | Nature, 2018, v. 559, p. 217-222 How to Cite? |
Abstract | The six-subunit origin recognition complex (ORC) binds to DNA to mark the site for the initiation of replication in eukaryotes. Here we report a 3 Å cryo-electron microscopy structure of the Saccharomyces cerevisiae ORC bound to a 72-base-pair origin DNA sequence that contains the ARS consensus sequence (ACS) and the B1 element. The ORC encircles DNA through extensive interactions with both phosphate backbone and bases, and bends DNA at the ACS and B1 sites. Specific recognition of thymine residues in the ACS is carried out by a conserved basic amino acid motif of Orc1 in the minor groove, and by a species-specific helical insertion motif of Orc4 in the major groove. Moreover, similar insertions into major and minor grooves are also embedded in the B1 site by basic patch motifs from Orc2 and Orc5, respectively, to contact bases and to bend DNA. This work pinpoints a conserved role of ORC in modulating DNA structure to facilitate origin selection and helicase loading in eukaryotes. |
Persistent Identifier | http://hdl.handle.net/10722/259932 |
ISSN | 2023 Impact Factor: 50.5 2023 SCImago Journal Rankings: 18.509 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, N | - |
dc.contributor.author | Lam, W | - |
dc.contributor.author | Zhai, Y | - |
dc.contributor.author | Cheng, J | - |
dc.contributor.author | Cheng, E | - |
dc.contributor.author | Zhao, Y | - |
dc.contributor.author | Gao, N | - |
dc.contributor.author | Tye, B | - |
dc.date.accessioned | 2018-09-03T04:17:47Z | - |
dc.date.available | 2018-09-03T04:17:47Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Nature, 2018, v. 559, p. 217-222 | - |
dc.identifier.issn | 0028-0836 | - |
dc.identifier.uri | http://hdl.handle.net/10722/259932 | - |
dc.description.abstract | The six-subunit origin recognition complex (ORC) binds to DNA to mark the site for the initiation of replication in eukaryotes. Here we report a 3 Å cryo-electron microscopy structure of the Saccharomyces cerevisiae ORC bound to a 72-base-pair origin DNA sequence that contains the ARS consensus sequence (ACS) and the B1 element. The ORC encircles DNA through extensive interactions with both phosphate backbone and bases, and bends DNA at the ACS and B1 sites. Specific recognition of thymine residues in the ACS is carried out by a conserved basic amino acid motif of Orc1 in the minor groove, and by a species-specific helical insertion motif of Orc4 in the major groove. Moreover, similar insertions into major and minor grooves are also embedded in the B1 site by basic patch motifs from Orc2 and Orc5, respectively, to contact bases and to bend DNA. This work pinpoints a conserved role of ORC in modulating DNA structure to facilitate origin selection and helicase loading in eukaryotes. | - |
dc.language | eng | - |
dc.relation.ispartof | Nature | - |
dc.title | Structure of the origin recognition complex bound to DNA replication origin | - |
dc.type | Article | - |
dc.identifier.email | Zhai, Y: zhai@hku.hk | - |
dc.identifier.authority | Zhai, Y=rp02398 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1038/s41586-018-0293-x | - |
dc.identifier.scopus | eid_2-s2.0-85049837013 | - |
dc.identifier.hkuros | 288595 | - |
dc.identifier.volume | 559 | - |
dc.identifier.spage | 217 | - |
dc.identifier.epage | 222 | - |
dc.identifier.eissn | 1476-4687 | - |
dc.identifier.isi | WOS:000438240900048 | - |
dc.identifier.f1000 | 733577384 | - |
dc.identifier.issnl | 0028-0836 | - |