QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 1 September 2005
doi: 10.1242/jcs.02556

This Article Figures Only Full Text Full Text (PDF) Supplementary Material An erratum has been published All Versions of this Article: jcs.02556v1 118/18/4261    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Petkovic, M. Articles by Stagljar, I. Search for Related Content PubMed PubMed Citation Articles by Petkovic, M. Articles by Stagljar, I. Social Bookmarking                         What's this?

The human Rothmund-Thomson syndrome gene product, RECQL4, localizes to distinct nuclear foci that coincide with proteins involved in the maintenance of genome stability

Maja Petkovic¹, Tobias Dietschy¹, Raimundo Freire², Renjie Jiao^1,* and Igor Stagljar^1,,

¹ Institute of Vet. Biochemistry and Molecular Biology, University of Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland
² Unidad de investigacion, Hospital Universitario de Canarias, Ofra s/n, La Cuesta, 38071 Tenerife, Spain

Author for correspondence (e-mail: stagljar{at}utoronto.ca)

Accepted 14 June 2005

Rothmund-Thomson syndrome (RTS) is a human genetic disorder characterized by genome instability, cancer susceptibility and premature aging. The gene defective in a subset of RTS cases, RECQL4, encodes a member of the RecQ family of DNA helicases. To better define the function of the RECQL4 protein, we have determined its subcellular localization. We have raised antibodies against the N- and C-terminal parts of RECQL4 and could show that in various human cells endogenous RECQL4 forms discrete nuclear foci that colocalize with promyelotic leukaemia protein (PML). The number of foci and their colocalization with PML does not significantly change after induction of different types of DNA damages. Silencing of RECQL4 expression by siRNA causes a significant reduction in RECQL4 nuclear foci formation. Furthermore, we demonstrate that RECQL4 foci coincide with foci formed by human Rad51 and regions of single-stranded DNA after induction of DNA double-strand breaks. In agreement with this, we also show that RECQL4 and Rad51 form a complex in human cells. Our findings suggest a role for RECQL4 in the repair of DNA double-strand breaks by homologous recombination and shed new light onto RECQL4's function in human cells.

Key words: Genome stability, Rothmund-Thomson syndrome (RTS), RecQ helicases, Immunofluorescence, Promyelotic leukaemia protein (PML), Rad51

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				C. Capp, J. Wu, and T.-s. Hsieh Drosophila RecQ4 Has a 3'-5' DNA Helicase Activity That Is Essential for Viability J. Biol. Chem., November 6, 2009; 284(45): 30845 - 30852. [Abstract] [Full Text] [PDF]

				S. H. Schurman, M. Hedayati, Z. Wang, D. K. Singh, E. Speina, Y. Zhang, K. Becker, M. Macris, P. Sung, D. M. Wilson III, et al. Direct and indirect roles of RECQL4 in modulating base excision repair capacity Hum. Mol. Genet., September 15, 2009; 18(18): 3470 - 3483. [Abstract] [Full Text] [PDF]

				T. Suzuki, T. Kohno, and Y. Ishimi DNA Helicase Activity in Purified Human RECQL4 Protein J. Biochem., September 1, 2009; 146(3): 327 - 335. [Abstract] [Full Text] [PDF]

				T. Dietschy, I. Shevelev, J. Pena-Diaz, D. Huhn, S. Kuenzle, R. Mak, M. F. Miah, D. Hess, M. Fey, M. O. Hottiger, et al. p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization J. Cell Sci., April 15, 2009; 122(8): 1258 - 1267. [Abstract] [Full Text] [PDF]

				W. Fan and J. Luo RecQ4 Facilitates UV Light-induced DNA Damage Repair through Interaction with Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A (XPA) J. Biol. Chem., October 24, 2008; 283(43): 29037 - 29044. [Abstract] [Full Text] [PDF]

				N. Selak, C. Z. Bachrati, I. Shevelev, T. Dietschy, B. van Loon, A. Jacob, U. Hubscher, J. D. Hoheisel, I. D. Hickson, and I. Stagljar The Bloom's syndrome helicase (BLM) interacts physically and functionally with p12, the smallest subunit of human DNA polymerase {delta} Nucleic Acids Res., September 1, 2008; 36(16): 5166 - 5179. [Abstract] [Full Text] [PDF]

				R. M. Brosh Jr and V. A. Bohr Human premature aging, DNA repair and RecQ helicases Nucleic Acids Res., December 3, 2007; 35(22): 7527 - 7544. [Abstract] [Full Text] [PDF]

				V. A. Rao, C. Conti, J. Guirouilh-Barbat, A. Nakamura, Z.-H. Miao, S. L. Davies, B. Sacca, I. D. Hickson, A. Bensimon, and Y. Pommier Endogenous {gamma}-H2AX-ATM-Chk2 Checkpoint Activation in Bloom's Syndrome Helicase Deficient Cells Is Related to DNA Replication Arrested Forks Mol. Cancer Res., July 1, 2007; 5(7): 713 - 724. [Abstract] [Full Text] [PDF]

				K. H. Schmidt, J. Wu, and R. D. Kolodner Control of Translocations between Highly Diverged Genes by Sgs1, the Saccharomyces cerevisiae Homolog of the Bloom's Syndrome Protein. Mol. Cell. Biol., July 1, 2006; 26(14): 5406 - 5420. [Abstract] [Full Text] [PDF]