NDLI: Handoff from recombinase to replisome: insights from transposition.

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Handoff from recombinase to replisome: insights from transposition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jones, J. M. Nakai, H. Doseeva, V.
Description	Author Affiliation: Nakai H ( Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, 331 Basic Science Building, 3900 Reservoir Road NW, Washington, DC 20007, USA. nakai@bc.georgetown.edu);
Abstract	Bacteriophage Mu replicates as a transposable element, exploiting host enzymes to promote initiation of DNA synthesis. The phage-encoded transposase MuA, assembled into an oligomeric transpososome, promotes transfer of Mu ends to target DNA, creating a fork at each end, and then remains tightly bound to both forks. In the transition to DNA synthesis, the molecular chaperone ClpX acts first to weaken the transpososome's interaction with DNA, apparently activating its function as a molecular matchmaker. This activated transpososome promotes formation of a new nucleoprotein complex (prereplisome) by yet unidentified host factors [Mu replication factors (MRF alpha 2)], which displace the transpososome in an ATP-dependent reaction. Primosome assembly proteins PriA, PriB, DnaT, and the DnaB--DnaC complex then promote the binding of the replicative helicase DnaB on the lagging strand template of the Mu fork. PriA helicase plays an important role in opening the DNA duplex for DnaB binding, which leads to assembly of DNA polymerase III holoenzyme to form the replisome. The MRF alpha 2 transition factors, assembled into a prereplisome, not only protect the fork from action by nonspecific host enzymes but also appear to aid in replisome assembly by helping to activate PriA's helicase activity. They consist of at least two separable components, one heat stable and the other heat labile. Although the MRF alpha 2 components are apparently not encoded by currently known homologous recombination genes such as recA, recF, recO, and recR, they may fulfill an important function in assembling replisomes on arrested replication forks and products of homologous strand exchange.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage Mu Genetics DNA Nucleotidyltransferases Metabolism DNA Replication DNA, Viral Biosynthesis Integrases Adenosine Triphosphatases Physiology DNA Helicases Recombinases Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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