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PMID: 12727519 Published · ppublish English Journal Article Review

Actin's prokaryotic homologs.

Current opinion in structural biology ·Vol. 13 ·No. 2 ·2003-04-00 ·Pages 244-8

Egelman EH

Abstract

Actin is one of the most abundant and conserved eukaryotic proteins. Remarkably, two prokaryotic homologs of actin, MreB and ParM, have only recently been identified. MreB and ParM polymerize into filaments and play important roles in the control of bacterial cell shape and plasmid segregation, respectively. Whereas the eukaryotic actins display a remarkable degree of conservation (e.g. no amino acid changes in muscle actin from chickens to humans), the two bacterial proteins have as much sequence similarity to each other ( approximately 11% sequence identity) as they do to actin. It is possible that the interesting properties of eukaryotic F-actin may account for the unusual degree of conservation among the actins, whereas the bacterial proteins have had fewer constraints over the course of evolution.

MeSH Terms
Actins/chemistry,classification,genetics,metabolism Amino Acid Sequence Animals Conserved Sequence Escherichia coli Proteins/chemistry,genetics,metabolism Evolution, Molecular Humans Molecular Sequence Data Prokaryotic Cells/chemistry,metabolism Protein Conformation Sequence Homology Species Specificity
Chemicals
Actins Escherichia coli Proteins ParM protein, E coli MreB protein, E coli
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Egelman Edward H
Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Box 800733, Charlottesville 22908-0733, USA. egelman@virginia.edu
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2003-04-00
Pages
244-8
Language
English
Region
England
NLM ID
9107784
Subset
IM
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