Conservation of Eubacterial Replicases
Authors:
Gene Wijffels a;
Brian Dalrymple a;
Kritaya Kongsuwan a;
Nicholas E. Dixon b
| Affiliations: | a CSIRO Livestock Industries, Queensland Bioscience Precinct, St. Lucia, Queensland |
| b Research School of Chemistry, Australian National University, Canberra, ACT, Australia |
DOI:
10.1080/15216540500138246
Publication Frequency:
12 issues per year
Subjects:
Cell Biology;
Molecular Biology;
Number of References: 39
Formats available:
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(English)
Previously published as:
Biochemistry and Molecular Biology International
(1039-9712)
until 1998
The circumstances under which this title is published have changed:
Reason for change: Changed publisher
Now published by: Wiley-Blackwell Publishing Ltd
Date of change: 2008
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Abstract
The last 15 years of effort in understanding bacterial DNA replication and repair has identified that the donut shaped β2 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 β dimer. In every case, binding of β2 by the polymerase enhances their processivity of DNA synthesis. This binding site is also the same point of interaction between β2 and the clamp loader complex, which binds β2, opens and places it onto the DNA strand and then vacates the site. β2 may also be involved in the initiation of DNA replication again via contact through this same site. While much of the research effort has focused on Escherichia coli and Bacillus subtilis, conservation of this complex system is becoming apparent in diverse bacteria.
IUBMB Life, 57: 413-419, 2005 |
| Keywords: Bacterial DNA replication; sliding clamp; clamp loader; DNA polymerase |
| view references (39) : view citations |

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