Subcellular structures of mycoplasmas

被引:18
作者
Balish, Mitchell F. [1 ]
机构
[1] Miami Univ, Dept Microbiol, Oxford, OH 45056 USA
来源
FRONTIERS IN BIOSCIENCE-LANDMARK | 2006年 / 11卷
关键词
mycoplasma; adherence; ultrastructure; attachment organelle; cytoskeleton; review;
D O I
10.2741/1943
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Although the field of prokaryotic cell biology is well-advanced now, mycoplasmas were the first bacteria in which the existence of a cytoskeleton was postulated. Despite this head-start, the cytoskeletons of mycoplasmas are presently less well understood than those of other bacteria. This deficit is principally attributable to three factors: the novel nature of most of the cytoskeletal elements as compared with other bacteria, which have the advantage of being related to eukaryotic cytoskeletal proteins; differences among the cytoskeletons of different mycoplasma species; and the fastidiousness of mycoplasmas, which complicates efforts to perform protein biochemistry. In better studied mycoplasmas like Mycoplasma pneumoniae, a major component of the cytoskeleton is associated with the attachment organelle, a polar structure that is essential for adherence to host cells, involved in gliding motility, and associated with cell division. Mycoplasma mobile also has structures that appear to be involved in gliding motility, though in contrast to the structures of M. pneumoniae, these are extracellular. Some other species also have distinct subcellular structures.
引用
收藏
页码:2017 / 2027
页数:11
相关论文
共 120 条
[1]   Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin [J].
Alvarez, RA ;
Blaylock, MW ;
Baseman, JB .
MOLECULAR MICROBIOLOGY, 2003, 48 (05) :1417-1425
[2]   A MOTILE ORGANISM OF THE PLEUROPNEUMONIA GROUP [J].
ANDREWES, CH ;
WELCH, FV .
JOURNAL OF PATHOLOGY AND BACTERIOLOGY, 1946, 58 (03) :578-&
[3]  
[Anonymous], MOL BIOL PATHOGENICI
[4]   The bacterial cytoskeleton: An intermediate filament-like function [J].
Ausmees, N ;
Kuhn, JR ;
Jacobs-Wagner, C .
CELL, 2003, 115 (06) :705-713
[5]   Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae [J].
Balish, MF ;
Ross, SM ;
Fisseha, M ;
Krause, DC .
MOLECULAR MICROBIOLOGY, 2003, 50 (05) :1507-1516
[6]   Localization of Mycoplasma pneumoniae cytadherence-associated protein HMW2 by fusion with green fluorescent protein:: implications for attachment organelle structure [J].
Balish, MF ;
Santurri, RT ;
Ricci, AM ;
Lee, KK ;
Krause, DC .
MOLECULAR MICROBIOLOGY, 2003, 47 (01) :49-60
[7]   Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell [J].
Balish, MF ;
Hahn, TW ;
Popham, PL ;
Krause, DC .
JOURNAL OF BACTERIOLOGY, 2001, 183 (12) :3680-3688
[8]   MOLECULAR-BASIS FOR CYTADSORPTION OF MYCOPLASMA-PNEUMONIAE [J].
BASEMAN, JB ;
COLE, RM ;
KRAUSE, DC ;
LEITH, DK .
JOURNAL OF BACTERIOLOGY, 1982, 151 (03) :1514-1522
[9]  
BASEMAN JB, 1987, ISRAEL J MED SCI, V23, P474
[10]   Transcriptional analysis of the conserved ftsZ gene cluster in Mycoplasma genitalium and Mycoplasma pneumoniae [J].
Benders, GA ;
Powell, BC ;
Hutchison, CA .
JOURNAL OF BACTERIOLOGY, 2005, 187 (13) :4542-4551