Title

Actin-related proteins (Arps): conformational switches for chromatin-remodeling machines

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine

Date

7-6-2000

Document Type

Article

Medical Subject Headings

Actins; Adenosine Triphosphatases; Amino Acid Sequence; Animals; Chromatin; Models, Biological; Models, Molecular; Protein Conformation

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: Bioessays. 2000 Jul;22(7):666-72. Link to article on publisher's site

Related Resources

Link to article in PubMed

PubMed ID

10878579