The structure and function of bacterial actin homologs.
During the past decade, the appreciation and understanding of how bacterial cells can be organized in both space and time have been revolutionized by the identification and characterization of multiple bacterial homologs of the eukaryotic actin cytoskeleton. Some of these bacterial actins, such as the plasmid-borne ParM protein, have highly specialized functions, whereas other bacterial actins, such as the chromosomally encoded MreB protein, have been implicated in a wide array of cellular activities. In this review we cover our current understanding of the structure, assembly, function, and regulation of bacterial actins. We focus on ParM as a well-understood reductionist model and on MreB as a central organizer of multiple aspects of bacterial cell biology. We also discuss the outstanding puzzles in the field and possible directions where this fast-developing area may progress in the future.
Shaevitz
Joshua W
JW
Department of Physics, Princeton University, Princeton, New Jersey 08544, USA.
Gitai
Zemer
Z
D000199:Actins / Q000502:physiology* / Q000648:ultrastructure; D001419:Bacteria / Q000378:metabolism / Q000648:ultrastructure; D018407:Bacterial Physiological Phenomena; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000502:physiology* / Q000648:ultrastructure; D010957:Plasmids / Q000502:physiology; D058105:Polymerization
D000199:Actins; D029968:Escherichia coli Proteins; C471255:ParM protein, E coli; C078473:MreB protein, E coli