AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

Neuwald, A. F., Aravind, L., Spouge, J. L., Koonin, E. V. (January 1999) AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Research, 9 (1). pp. 27-43. ISSN 1088-9051 (Print)

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URL: http://www.ncbi.nlm.nih.gov/pubmed/9927482
DOI: 10.1101/gr.9.1.27

Abstract

Using a combination of computer methods for iterative database searches and multiple sequence alignment, we show that protein sequences related to the AAA family of ATPases are far more prevalent than reported previously. Among these are regulatory components of Lon and Clp proteases, proteins involved in DNA replication, recombination, and restriction (including subunits of the origin recognition complex, replication factor C proteins, MCM DNA-licensing factors and the bacterial DnaA, RuvB, and McrB proteins), prokaryotic NtrC-related transcription regulators, the Bacillus sporulation protein SpoVJ, Mg2+, and Co2+ chelatases, the Halobacterium GvpN gas vesicle synthesis protein, dynein motor proteins, TorsinA, and Rubisco activase. Alignment of these sequences, in light of the structures of the clamp loader delta' subunit of Escherichia coli DNA polymerase III and the hexamerization component of N-ethylmaleimide-sensitive fusion protein, provides structural and mechanistic insights into these proteins, collectively designated the AAA+ class. Whole-genome analysis indicates that this class is ancient and has undergone considerable functional divergence prior to the emergence of the major divisions of life. These proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes. The hexameric architecture often associated with this class can provide a hole through which DNA or RNA can be thread; this may be important for assembly or remodeling of DNA-protein complexes.

Item Type: Paper
Uncontrolled Keywords: Adenosinetriphosphatase/ chemistry/ classification/metabolism Amino Acid Sequence Animals Computational Biology Conserved Sequence Databases, Factual Dimerization Humans Models, Molecular Molecular Chaperones/ chemistry/ classification/metabolism Molecular Sequence Data Peptide Fragments/chemistry/classification/metabolism Protein Conformation Proteins/ metabolism Research Support, U.S. Gov't, P.H.S. Sequence Alignment
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > alignment > sequence alignment
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > ATPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > chaperones
CSHL Authors:
Communities: CSHL labs > Neuwald lab
Depositing User: Kathleen Darby
Date: January 1999
Date Deposited: 30 Apr 2014 15:45
Last Modified: 30 Apr 2014 15:45
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29791

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