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Molecular and Cellular Biology, February 2008, p. 1197-1206, Vol. 28, No. 4
0270-7306/08/$08.00+0     doi:10.1128/MCB.00767-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification of the Proteins, Including MAGEG1, That Make Up the Human SMC5-6 Protein Complex{triangledown}

Elaine M. Taylor, Alice C. Copsey, Jessica J. R. Hudson, Susanne Vidot, and Alan R. Lehmann*

Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom

Received 2 May 2007/ Returned for modification 20 June 2007/ Accepted 19 November 2007

The SMC protein complexes play important roles in chromosome dynamics. The function of the SMC5-6 complex remains unclear, though it is involved in resolution of different DNA structures by recombination. We have now identified and characterized the four non-SMC components of the human complex and in particular demonstrated that the MAGEG1 protein is part of this complex. MAGE proteins play important but as yet undefined roles in carcinogenesis, apoptosis, and brain development. We show that, with the exception of the SUMO ligase hMMS21/hNSE2, depletion of any of the components results in degradation of all the other components. Depletion also confers sensitivity to methyl methanesulfonate. Several of the components are modified by sumoylation and ubiquitination.


* Corresponding author. Mailing address: Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom. Phone: 44 1273 678120. Fax: 44 1273 678121. E-mail: a.r.lehmann{at}sussex.ac.uk

{triangledown} Published ahead of print on 17 December 2007.


Molecular and Cellular Biology, February 2008, p. 1197-1206, Vol. 28, No. 4
0270-7306/08/$08.00+0     doi:10.1128/MCB.00767-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




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  • Pebernard, S., Perry, J. J. P., Tainer, J. A., Boddy, M. N. (2008). Nse1 RING-like Domain Supports Functions of the Smc5-Smc6 Holocomplex in Genome Stability. Mol. Biol. Cell 19: 4099-4109 [Abstract] [Full Text]