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In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex

In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex
In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex
Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein-protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have used the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physical association between the DNA ligase IV polypeptide and the human condensin subunit known as hCAP-E. The hCAP-E polypeptide, a member of the Structural Maintenance of Chromosomes (SMC) super-family of proteins, coimmunoprecipitates from cell extracts with DNA ligase IV. Immunofluorescence studies reveal colocalization of DNA ligase IV and hCAP-E in the interphase nucleus, whereas mitotic cells display colocalization of both polypeptides on mitotic chromosomes. Strikingly, the XRCC4 protein is excluded from the area of mitotic chromosomes, suggesting the formation of specialized DNA ligase IV complexes subject to cell cycle regulation. We discuss our findings in light of known and hypothesized roles for ligase IV and the condensin complex.
1059-1524
685-697
Przewloka, Marcin
9b25e73c-ec15-43df-a5a4-ac9574bb20ab
Pardington, Paige E.
1dfc7c61-d60a-46f3-8c8c-8ba8e4b140b1
Yannone, Steven M.
5806344b-8936-4848-89c6-cc4084256281
Chen, David J.
100b5a5c-d20b-404b-9242-929f7bbb4bcd
Cary, Robert B.
41823d60-cf08-4626-a6f2-a0f85128324d
Przewloka, Marcin
9b25e73c-ec15-43df-a5a4-ac9574bb20ab
Pardington, Paige E.
1dfc7c61-d60a-46f3-8c8c-8ba8e4b140b1
Yannone, Steven M.
5806344b-8936-4848-89c6-cc4084256281
Chen, David J.
100b5a5c-d20b-404b-9242-929f7bbb4bcd
Cary, Robert B.
41823d60-cf08-4626-a6f2-a0f85128324d

Przewloka, Marcin, Pardington, Paige E., Yannone, Steven M., Chen, David J. and Cary, Robert B. (2003) In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex. Molecular Biology of the Cell, 14 (2), 685-697. (doi:10.1091/mbc.E01-11-0117). (PMID:12589063)

Record type: Article

Abstract

Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein-protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have used the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physical association between the DNA ligase IV polypeptide and the human condensin subunit known as hCAP-E. The hCAP-E polypeptide, a member of the Structural Maintenance of Chromosomes (SMC) super-family of proteins, coimmunoprecipitates from cell extracts with DNA ligase IV. Immunofluorescence studies reveal colocalization of DNA ligase IV and hCAP-E in the interphase nucleus, whereas mitotic cells display colocalization of both polypeptides on mitotic chromosomes. Strikingly, the XRCC4 protein is excluded from the area of mitotic chromosomes, suggesting the formation of specialized DNA ligase IV complexes subject to cell cycle regulation. We discuss our findings in light of known and hypothesized roles for ligase IV and the condensin complex.

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More information

Accepted/In Press date: 31 October 2002
e-pub ahead of print date: 18 November 2002
Published date: February 2003
Organisations: Molecular and Cellular, Centre for Biological Sciences

Identifiers

Local EPrints ID: 393868
URI: http://eprints.soton.ac.uk/id/eprint/393868
ISSN: 1059-1524
PURE UUID: 9f6f8491-e320-47e7-be4e-aca2fe8b25d2
ORCID for Marcin Przewloka: ORCID iD orcid.org/0000-0002-0329-9162

Catalogue record

Date deposited: 26 May 2016 11:29
Last modified: 20 Jul 2019 00:33

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