PMID:19833870
| Citation |
Miller, DT, Grimwade, JE, Betteridge, T, Rozgaja, T, Torgue, JJ and Leonard, AC (2009) Bacterial origin recognition complexes direct assembly of higher-order DnaA oligomeric structures. Proc. Natl. Acad. Sci. U.S.A. 106:18479-84 |
|---|---|
| Abstract |
Eukaryotic initiator proteins form origin recognition complexes (ORCs) that bind to replication origins during most of the cell cycle and direct assembly of prereplication complexes (pre-RCs) before the onset of S phase. In the eubacterium Escherichia coli, there is a temporally similar nucleoprotein complex comprising the initiator protein DnaA bound to three high-affinity recognition sites in the unique origin of replication, oriC. At the time of initiation, this high-affinity DnaA-oriC complex (the bacterial ORC) accumulates additional DnaA that interacts with lower-affinity sites in oriC, forming a pre-RC. In this paper, we investigate the functional role of the bacterial ORC and examine whether it mediates low-affinity DnaA-oriC interactions during pre-RC assembly. We report that E. coli ORC is essential for DnaA occupation of low-affinity sites. The assistance given by ORC is directed primarily to proximal weak sites and requires oligomerization-proficient DnaA. We propose that in bacteria, DnaA oligomers of limited length and stability emerge from single high-affinity sites and extend toward weak sites to facilitate their loading as a key stage of prokaryotic pre-RC assembly. |
| Links |
PubMed PMC2773971 Online version:10.1073/pnas.0909472106 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Escherichia coli/metabolism; Molecular Sequence Data; Mutation/genetics; Origin Recognition Complex/metabolism; Protein Binding; Protein Structure, Quaternary; Replication Origin/genetics |
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