Bimodal activation of SMC ATPase by intra- and inter-molecular interactions

Hirano, M., Anderson, D. E., Erickson, H. P., Hirano, T. (2001) Bimodal activation of SMC ATPase by intra- and inter-molecular interactions. Embo Journal, 20 (12). pp. 3238-3250. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/11406600
DOI: 10.1093/emboj/20.12.3238

Abstract

Structural maintenance of chromosomes (SMC) proteins play fundamental roles in higher-order chromosome dynamics from bacteria to humans, It has been proposed that the Bacillus subtilis SMC (BsSMC) homodimer is composed of two anti-parallel coiled-coil arms, each having an ATP-binding domain at its distal end. It remains totally unknown, however, how the two-armed structure supports ATP-dependent actions of BsSMC, By constructing a number of mutant derivatives including 'single-armed' BsSMC, we show here that the central hinge domain provides a structural flexibility that allows opening and closing of the two arms, This unique structure brings about bimodal regulation of the SMC ATPase cycle. Closing the arm can trigger ATP hydrolysis by allowing an end-end interaction within a dimer (intramolecular mode). When bound to DNA, ATP promotes a dimer-dimer interaction, which in turn activates their DNA-dependent ATPase activity (intermolecular mode). Our results reveal a novel mechanism of ATPase regulation and provide mechanistic insights into how eukaryotic SMC protein complexes could mediate diverse chromosomal functions, such as chromosome condensation and sister chromatid chromosome cohesion.

Item Type: Paper
Uncontrolled Keywords: Bacillus subtilis chromosome dynamics cohesin condensin structural maintenance of chromosomes MITOTIC CHROMOSOME CONDENSATION SISTER-CHROMATID COHESION SACCHAROMYCES-CEREVISIAE STRUCTURAL MAINTENANCE DOSAGE COMPENSATION PROTEIN COMPLEXES 13S CONDENSIN COILED COILS X-CHROMOSOME DNA
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > ATPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosome
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function > chromosome

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cohesin
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > condensin complex
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: Matt Covey
Date Deposited: 21 Jan 2014 16:02
Last Modified: 21 Jan 2014 16:02
PMCID: PMC150201
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29249

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