HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Fleck, O. Articles by Kohli, J. Search for Related Content PubMed PubMed Citation Articles by Fleck, O. Articles by Kohli, J. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 46, 30398-30405, November 13, 1998

The High Mobility Group Domain Protein Cmb1 of Schizosaccharomyces pombe Binds to Cytosines in Base Mismatches and Opposite Chemically Altered Guanines

From the Institute of General Microbiology, University of Bern, Baltzer-Strasse 4, CH-3012 Bern, Switzerland

The mismatch-binding activity Cmb1 of Schizosaccharomyces pombe was enriched from wild type cells, and N-terminal sequencing enabled cloning of the respective gene. The deduced amino acid sequence of cmb1⁺ contains a high mobility group domain, a motif that is common to a heterogeneous family of DNA-binding proteins. In crude protein extracts of a cmb1 gene-disruption strain, specific binding to C/T, C/A, and C/ was abolished. Weak binding to C/C revealed the presence of a second mismatch-binding activity, Cmb2. Cmb1, enriched from S. pombe and purified from Escherichia coli, bound specifically to C/C, C/T, C/A, T/T, and C/ but showed little or no affinity to other mismatches and small loops. Cmb1 recognizes 1,2 GpG intrastrand cross-links, produced by the chemotherapeutic drug cisplatin, when two cytosines are opposite the cross-linked guanines but not when other bases are present. Consistently, O⁶-methylguanine:C but not O⁶-methylguanine/T lesions were bound. Thus, cytosines in mismatches and opposite chemically modified guanines are the preferred target of Cmb1 recognition. cmb1 mutant cells are more sensitive to cisplatin than wild type cells, indicating a role of Cmb1 in repair of cisplatin-induced DNA damage.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				R. Muheim-Lenz, T. Buterin, G. Marra, and H. Naegeli Short-patch correction of C/C mismatches in human cells Nucleic Acids Res., December 21, 2004; 32(22): 6696 - 6705. [Abstract] [Full Text] [PDF]

				F. Yuan, L. Gu, S. Guo, C. Wang, and G.-M. Li Evidence for Involvement of HMGB1 Protein in Human DNA Mismatch Repair J. Biol. Chem., May 14, 2004; 279(20): 20935 - 20940. [Abstract] [Full Text] [PDF]

				P. Perego, G. S. Jimenez, L. Gatti, S. B. Howell, and F. Zunino Yeast Mutants As a Model System for Identification of Determinants of Chemosensitivity Pharmacol. Rev., December 1, 2000; 52(4): 477 - 492. [Abstract] [Full Text] [PDF]

				T. Nakahara, Q.-M. Zhang, K. Hashiguchi, and S. Yonei Identification of proteins of Escherichia coli and Saccharomyces cerevisiae that specifically bind to C/C mismatches in DNA Nucleic Acids Res., July 1, 2000; 28(13): 2551 - 2556. [Abstract] [Full Text] [PDF]

				A. T. Yarnell, S. Oh, D. Reinberg, and S. J. Lippard Interaction of FACT, SSRP1, and the High Mobility Group (HMG) Domain of SSRP1 with DNA Damaged by the Anticancer Drug Cisplatin J. Biol. Chem., July 6, 2001; 276(28): 25736 - 25741. [Abstract] [Full Text] [PDF]

				M. Hohl, O. Christensen, C. Kunz, H. Naegeli, and O. Fleck Binding and Repair of Mismatched DNA Mediated by Rhp14, the Fission Yeast Homologue of Human XPA J. Biol. Chem., August 10, 2001; 276(33): 30766 - 30772. [Abstract] [Full Text] [PDF]