Extracellular biology of Myxococcus xanthus

被引:129
作者
Konovalova, Anna [1 ]
Petters, Tobias [1 ]
Sogaard-Andersen, Lotte [1 ]
机构
[1] Max Planck Inst Terr Microbiol, Dept Ecophysiol, D-35043 Marburg, Germany
关键词
Myxococcus xanthus; extracellular matrix; protein secretion; bacterial motility; secondary metabolism; contact-dependent activity; DEVELOPMENTAL GENE-EXPRESSION; FRUITING BODY MORPHOGENESIS; SOCIAL GLIDING MOTILITY; IV PILI; VI SECRETION; C-FACTOR; CELL-INTERACTIONS; PROTEIN TRANSLOCATION; CYTOPLASMIC-RECEPTOR; CHEMOTAXIS HOMOLOGS;
D O I
10.1111/j.1574-6976.2009.00194.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Myxococcus xanthus has a lifecycle characterized by several social interactions. In the presence of prey, M. xanthus is a predator forming cooperatively feeding colonies, and in the absence of nutrients, M. xanthus cells interact to form multicellular, spore-filled fruiting bodies. Formation of both cellular patterns depends on extracellular functions including the extracellular matrix and intercellular signals. Interestingly, the formation of these patterns also depends on several activities that involve direct cell-cell contacts between M. xanthus cells or direct contacts between M. xanthus cells and the substratum, suggesting that M. xanthus cells have a marked ability to distinguish self from nonself. Genome-wide analyses of the M. xanthus genome reveal a large potential for protein secretion. Myxococcus xanthus harbours all protein secretion systems required for translocation of unfolded and folded proteins across the cytoplasmic membrane and an intact type II secretion system. Moreover, M. xanthus contains 60 ATP-binding cassette transporters, two degenerate type III secretion systems, both of which lack the parts in the outer membrane and the needle structure, and an intact type VI secretion system for one-step translocation of proteins across the cell envelope. Also, analyses of the M. xanthus proteome reveal a large protein secretion potential including many proteins of unknown function.
引用
收藏
页码:89 / 106
页数:18
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