Opening closed arms: long-distance activation of SMC ATPase by hinge-DNA interactions

Hirano, M., Hirano, T. (2006) Opening closed arms: long-distance activation of SMC ATPase by hinge-DNA interactions. Mol Cell, 21 (2). pp. 175-86. ISSN 1097-2765 (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/16427008
DOI: 10.1016/j.molcel.2005.11.026

Abstract

Structural maintenance of chromosomes (SMC) proteins form a V-shaped dimer in which a central hinge domain connects two coiled-coil arms, each having an ATP binding head domain at its distal end. Here, we show that the hinge domain plays essential roles in modulating the mechanochemical cycle of SMC proteins. An initial interaction of the hinge domain with DNA leads to opening of the arms by triggering hydrolysis of ATP bound to the head domains, which are located approximately 50 nm away from the hinge. This conformational change allows the inner surface of the hinge domain to stably interact with DNA by an ATP-independent mechanism and primes ATP-driven engagement between the liberated head domains either intramolecularly or intermolecularly. Consistently, a variety of hinge mutations drastically alter DNA binding properties of SMC proteins through distinct mechanisms. Our results suggest that SMC proteins possess an intrinsic property to change their own conformations upon binding to DNA.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphatases chemistry genetics metabolism Adenosine Triphosphate metabolism Amino Acid Sequence Archaeal Proteins chemistry genetics metabolism Bacterial Proteins chemistry genetics metabolism Binding Sites genetics Chromosomal Proteins Non-Histone chemistry genetics metabolism DNA metabolism Enzyme Activation Humans Kinetics Models Biological Models Molecular Molecular Sequence Data Point Mutation Protein Structure Tertiary Recombinant Proteins chemistry genetics metabolism Sequence Homology Amino Acid
Subjects: bioinformatics > genomics and proteomics > design > protein design
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
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: CSHL Librarian
Date Deposited: 13 Dec 2011 18:56
Last Modified: 16 Apr 2018 21:23
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22818

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