Nucleic Acids Research Advance Access first published online on September 26, 2006
This version published online on October 5, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl677
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Human RECQ5ß helicase promotes strand exchange on synthetic DNA structures resembling a stalled replication fork
Institute of Molecular Cancer Research, University of Zurich Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
*To whom correspondence should be addressed. Tel: +41 44 635 3470; Fax: +41 44 635 3484; Email: pjanscak{at}imcr.unizh.ch
Received July 25, 2006. Revised August 30, 2006. Accepted September 4, 2006.
The role of the human RECQ5ß helicase in the maintenance of genomic stability remains elusive. Here we show that RECQ5ß promotes strand exchange between arms of synthetic forked DNA structures resembling a stalled replication fork in a reaction dependent on ATP hydrolysis. BLM and WRN can also promote strand exchange on these structures. However, in the presence of human replication protein A (hRPA), the action of these RecQ-type helicases is strongly biased towards unwinding of the parental duplex, an effect not seen with RECQ5ß. A domain within the non-conserved portion of RECQ5ß is identified as being important for its ability to unwind the lagging-strand arm and to promote strand exchange on hRPA-coated forked structures. We also show that RECQ5ß associates with DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks after exposure of cells to UV irradiation. Moreover, RECQ5ß is found to physically interact with the polymerase processivity factor proliferating cell nuclear antigen in vitro and in vivo. Collectively, these findings suggest that RECQ5ß may promote regression of stalled replication forks to facilitate the bypass of replication-blocking lesions by template-switching. Loss of such activity could explain the elevated level of mitotic crossovers observed in RECQ5ß-deficient cells.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  D. Kobbe, S. Blanck, M. Focke, and H. Puchta Biochemical Characterization of AtRECQ3 Reveals Significant Differences Relative to Other RecQ Helicases Plant Physiology, November 1, 2009; 151(3): 1658 - 1666. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. George, Q. Wen, R. Griffiths, A. Ganesh, M. Meuth, and C. M. Sanders Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks Nucleic Acids Res., October 1, 2009; 37(19): 6491 - 6502. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. Aygun, X. Xu, Y. Liu, H. Takahashi, S. E. Kong, R. C. Conaway, J. W. Conaway, and J. Q. Svejstrup Direct Inhibition of RNA Polymerase II Transcription by RECQL5 J. Biol. Chem., August 28, 2009; 284(35): 23197 - 23203. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Atkinson and P. McGlynn Replication fork reversal and the maintenance of genome stability Nucleic Acids Res., June 1, 2009; 37(11): 3475 - 3492. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Zheng, R. Kanagaraj, B. Mihaljevic, S. Schwendener, A. A. Sartori, B. Gerrits, I. Shevelev, and P. Janscak MRE11 complex links RECQ5 helicase to sites of DNA damage Nucleic Acids Res., May 1, 2009; 37(8): 2645 - 2657. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Hu, X. Lu, G. Zhou, E. L. Barnes, and G. Luo Recql5 Plays an Important Role in DNA Replication and Cell Survival after Camptothecin Treatment Mol. Biol. Cell, January 1, 2009; 20(1): 114 - 123. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Gu, Y. Masuda, and K. Kamiya Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain Nucleic Acids Res., November 1, 2008; 36(19): 6295 - 6308. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. Aygun, J. Svejstrup, and Y. Liu A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin PNAS, June 24, 2008; 105(25): 8580 - 8584. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. Li, S. Lu, G. Hou, X. Ma, D. Sheng, J. Ni, and Y. Shen Hjm/Hel308A DNA Helicase from Sulfolobus tokodaii Promotes Replication Fork Regression and Interacts with Hjc Endonuclease In Vitro J. Bacteriol., April 15, 2008; 190(8): 3006 - 3017. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Branzei and M. Foiani RecQ helicases queuing with Srs2 to disrupt Rad51 filaments and suppress recombination Genes & Dev., December 1, 2007; 21(23): 3019 - 3026. [Full Text] [PDF]
|
|
|
|
|
|
Y. Hu, S. Raynard, M. G. Sehorn, X. Lu, W. Bussen, L. Zheng, J. M. Stark, E. L. Barnes, P. Chi, P. Janscak, et al. RECQL5/Recql5 helicase regulates homologous recombination and suppresses tumor formation via disruption of Rad51 presynaptic filaments Genes & Dev., December 1, 2007; 21(23): 3073 - 3084. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Machwe, L. Xiao, R. G. Lloyd, E. Bolt, and D. K. Orren Replication fork regression in vitro by the Werner syndrome protein (WRN): Holliday junction formation, the effect of leading arm structure and a potential role for WRN exonuclease activity Nucleic Acids Res., September 27, 2007; 35(17): 5729 - 5747. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
O. N. Voloshin and R. D. Camerini-Otero The DinG Protein from Escherichia coli Is a Structure-specific Helicase J. Biol. Chem., June 22, 2007; 282(25): 18437 - 18447. [Abstract] [Full Text] [PDF]
|
|