2005
DOI: 10.1080/15216540500138246
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Conservation of Eubacterial Replicases

Abstract: SummaryThe last 15 years of effort in understanding bacterial DNA replication and repair has identified that the donut shaped b 2 sliding clamp is harnessed by very functionally different DNA polymerases throughout the lifecycle of the bacterial cell. Remarkably, the sites of binding of these polymerases, in most cases, appear to be the same shallow pocket on the b dimer. In every case, binding of b 2 by the polymerase enhances their processivity of DNA synthesis. This binding site is also the same point of in… Show more

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Cited by 44 publications
(29 citation statements)
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“…The hydrophobic groove on the ␤ sliding clamp and its binding motifs in other proteins are strongly conserved across bacterial species (27,260). An analogous mechanism is also shared by the PCNA sliding clamp of archaea and eukaryotes (209), although the consensus sequence recognized by PCNA (QxxLxxFF) is different from that of the bacterial ␤-binding motifs (55).…”
Section: Highly Conserved Protein Interaction Modules Within the ␤ Slmentioning
confidence: 87%
See 1 more Smart Citation
“…The hydrophobic groove on the ␤ sliding clamp and its binding motifs in other proteins are strongly conserved across bacterial species (27,260). An analogous mechanism is also shared by the PCNA sliding clamp of archaea and eukaryotes (209), although the consensus sequence recognized by PCNA (QxxLxxFF) is different from that of the bacterial ␤-binding motifs (55).…”
Section: Highly Conserved Protein Interaction Modules Within the ␤ Slmentioning
confidence: 87%
“…In addition to binding the Pol III ␦ subunit during clamp loading/unloading (127) and the ␣ polymerase subunit (261), greatly increasing its processivity, the E. coli ␤ sliding clamp also binds to DNA polymerases I, II, IV, and V; DNA ligase; Hda; and the mismatch repair proteins MutS and MutL (55,159,260). Each of these proteins binds to a hydrophobic groove (127) hexameric peptide motif, which is often located close to the N or C terminus (55).…”
Section: Highly Conserved Protein Interaction Modules Within the ␤ Slmentioning
confidence: 99%
“…Recent studies have shown, however, that the function of the sliding clamp is not limited to serving as a subunit of the replicative DNA polymerase [1][2][3][4]13]. In E. coli, the β sliding clamp is found to also play a role in okazaki fragment maturation by interacting with DNA ligase and DNA polymerase I [14].…”
Section: Introductionmentioning
confidence: 99%
“…The dnaN gene of Escherichia coli encodes the β subunit of E. coli DNA polymerase III [1][2][3][4]. The β subunit dimerizes to form a ring-shaped sliding clamp, which encircles an intact duplex DNA and moves freely on it [5,6].…”
Section: Introductionmentioning
confidence: 99%
“…The main focus of this review will be on the mechanism of loading the Escherichia coli sliding clamp onto DNA, with special emphasis on the dynamic and transient interactions that are required to catalyze the reaction. Reviews on the complete replisomes and clamp loaders from E. coli (Johnson and O'Donnell, 2005;Marians, 2004;McHenry, 2003;Wijffels et al, 2005), bacteriophage T4 Trakselis and Benkovic, 2001;Trakselis et al, 2001b), and eukaryotes (Bell and Dutta, 2002;Garg and Burgers, 2005;Johnson and O'Donnell, 2005;Kao and Bambara, 2003;Majka and Burgers, 2004;Waga and Stillman, 1998) have been published recently.…”
Section: Introductionmentioning
confidence: 99%