A single domain of the replication termination protein of Bacillus subtilis is involved in arresting both DnaB helicase and RNA polymerase

The Journal of Biological Chemistry
A GautamD Bastia

Abstract

The current models that have been proposed to explain the mechanism of replication termination are (i) passive arrest of a replication fork by the terminus (Ter) DNA-terminator protein complex that impedes the replication fork and the replicative helicase in a polar fashion and (ii) an active barrier model in which the Ter-terminator protein complex arrests a fork not only by DNA-protein interaction but also by mechanistically significant terminator protein-helicase interaction. Despite the existence of some evidence supporting in vitro interaction between the replication terminator protein (RTP) and DnaB helicase, there has been continuing debate in the literature questioning the validity of the protein-protein interaction model. The objective of the present work was two-fold: (i) to reexamine the question of RTP-DnaB interaction by additional techniques and different mutant forms of RTP, and (ii) to investigate if a common domain of RTP is involved in the arrest of both helicase and RNA polymerase. The results validate and confirm the RTP-DnaB interaction in vitro and suggest a critical role for this interaction in replication fork arrest. The results also show that the Tyr(33) residue of RTP plays a critical role both in the...Continue Reading

References

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Citations

Aug 19, 2008·Proceedings of the National Academy of Sciences of the United States of America·Deepak BastiaMarc M Greenberg
Aug 9, 2001·Proceedings of the National Academy of Sciences of the United States of America·S MuluguD Bastia
Apr 5, 2003·Molecular Microbiology·Marat SadykovIchizo Kobayashi
Mar 21, 2009·Molecular Microbiology·Daniel L Kaplan, Deepak Bastia
Nov 21, 2008·Molecular Microbiology·Iain G DugginThomas M Hill

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