Hirano, M., Anderson, D. E., Erickson, H. P., Hirano, T.
(June 2001)
Bimodal activation of SMC ATPase by intra- and inter-molecular interactions.
Embo Journal, 20 (12).
pp. 3238-3250.
ISSN 0261-4189
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
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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: |
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Communities: |
CSHL labs > Hirano lab |
Depositing User: |
Matt Covey
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Date: |
June 2001 |
Date Deposited: |
21 Jan 2014 16:02 |
Last Modified: |
21 Jan 2014 16:02 |
PMCID: |
PMC150201 |
Related URLs: |
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URI: |
https://repository.cshl.edu/id/eprint/29249 |
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