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
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: | https://repository.cshl.edu/id/eprint/29898 |
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