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Actin‐related proteins (Arps): conformational switches for chromatin‐remodeling machines?
Author(s) -
Boyer Laurie A.,
Peterson Craig L.
Publication year - 2000
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/1521-1878(200007)22:7<666::aid-bies9>3.0.co;2-y
Subject(s) - cytoskeleton , chromatin remodeling , biology , actin remodeling , microbiology and biotechnology , actin , aaa proteins , chromatin , cofilin , actin binding protein , biochemistry , atpase , actin cytoskeleton , cell , enzyme , dna
The actin superfamily of ATPases includes cytoskeletal actins, the stress 70 proteins (e.g. hsc70), sugar kinases, glycerol kinase, and several prokaryotic cell cycle proteins. Although these proteins share limited sequence identity, they all appear to maintain a similar tertiary structure, the “actin fold”, which may serve to couple ATP hydrolysis to protein conformational changes. Recently, an actin‐related protein (Arp) subfamily has been identified based on sequence homology to conventional actin. Although some Arps are clearly involved in cytoskeletal functions, both actin and/or Arps have been found as stoichiometric subunits of several nuclear chromatin‐remodeling enzymes. Here we present two related models in which actin and/or Arps function as conformational switches that control either the activity or the assembly of chromatin‐remodeling machines. BioEssays 22:666–672, 2000. © 2000 John Wiley & Sons, Inc.