30 Apr 2004 18:9 AR AR214-BB33-09.tex AR214-BB33-09.sgm LaTeX2e(2002/01/18) P1: FHD 10.1146/annurev.biophys.33.110502.132647 Annu. Rev. Biophys. Biomol. Struct. 2004. 33:177–98 doi: 10.1146/annurev.biophys.33.110502.132647 Copyright c 2004 by Annual Reviews. All rights reserved First published online as a Review in Advance on January 7, 2004 MOLECULES OF THE BACTERIAL CYTOSKELETON Jan Lowe,¨ Fusinita van den Ent, and Linda A. Amos MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom; email:
[email protected];
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[email protected] Key Words FtsZ, MreB, ParM, tubulin, actin ■ Abstract The structural elucidation of clear but distant homologs of actin and tubulin in bacteria and GFP labeling of these proteins promises to reinvigorate the field of prokaryotic cell biology. FtsZ (the tubulin homolog) and MreB/ParM (the actin ho- mologs) are indispensable for cellular tasks that require the cell to accurately position molecules, similar to the function of the eukaryotic cytoskeleton. FtsZ is the organizing molecule of bacterial cell division and forms a filamentous ring around the middle of the cell. Many molecules, including MinCDE, SulA, ZipA, and FtsA, assist with this process directly. Recently, genes much more similar to tubulin than to FtsZ have been identified in Verrucomicrobia. MreB forms helices underneath the inner membrane and probably defines the shape of the cell by positioning transmembrane and periplas- mic cell wall–synthesizing enzymes. Currently, no interacting proteins are known for MreB and its relatives that help these proteins polymerize or depolymerize at certain times and places inside the cell.