ATP-dependent aggregation of single-stranded DNA by a bacterial SMC homodimer

Hirano, M., Hirano, T. (December 1998) ATP-dependent aggregation of single-stranded DNA by a bacterial SMC homodimer. Embo Journal, 17 (23). pp. 7139-48. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/9843517
DOI: 10.1093/emboj/17.23.7139

Abstract

SMC (structural maintenance of chromosomes) proteins are putative ATPases that are highly conserved among Bacteria, Archaea and Eucarya. Eukaryotic SMC proteins are implicated in a diverse range of chromosome dynamics including chromosome condensation, dosage compensation and recombinational repair. In eukaryotes, two different SMC proteins form a heterodimer, which in turn acts as the core component of a large protein complex. Despite recent progress, no ATP-dependent activity has been found in individual SMC subunits. We report here the first biochemical characterization of a bacterial SMC protein from Bacillus subtilis. Unlike eukaryotic versions, the B.subtilis SMC protein (BsSMC) is a simple homodimer with no associated subunits. It binds preferentially to single-stranded DNA (ssDNA) and has a ssDNA-stimulated ATPase activity. In the presence of ATP, BsSMC forms large nucleoprotein aggregates in a ssDNA-specific manner. Proteolytic cleavage of BsSMC is changed upon binding to ATP and ssDNA. The energy-dependent aggregation of ssDNA might represent a primitive type of chromosome condensation that occurs during segregation of bacterial chromosomes.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphate/ metabolism Adenosinetriphosphatase/genetics/isolation & purification/ metabolism Amino Acid Sequence Bacillus subtilis/ enzymology/genetics Bacterial Proteins/genetics/isolation & purification/ metabolism DNA, Single-Stranded/ metabolism DNA-Binding Proteins/genetics/isolation & purification/ metabolism Dimerization Endopeptidases/metabolism Molecular Sequence Data Research Support, Non-U.S. Gov't
Subjects: bioinformatics > genomics and proteomics > small molecules > ATP
bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: Kathleen Darby
Date: 1 December 1998
Date Deposited: 01 May 2014 18:37
Last Modified: 01 May 2014 18:37
PMCID: PMC1171060
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29898

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