Mycoplasma and bacterial proteins resembling contractile proteins: a review.
The basis of gliding motility in prokaryotes including certain mycoplasmas and the ability of mycoplasmas to retain their characteristic cell shapes in the absence of a supporting cell wall is unexplained. This review examines the available studies describing proteins resembling contractile proteins and cytoskeletal proteins in prokaryotes. Proteins with a significant degree of amino acid sequence homology to the myofibrillar proteins actin and myosin Al light chain and to tropomyosin have been described in prokaryotes. In addition, protein preparations from Mycoplasma pneumoniae have been shown to bind heavy meromyosin fragments, anti-actin antibody, and phalloidin; however, it remains to be proved that proteins in these preparations sharing properties with actin are synthesized by the mycoplasma.
D000199:Actins / Q000032:analysis / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis; D003285:Contractile Proteins / Q000032:analysis / Q000378:metabolism; D003572:Cytochalasins / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D009174:Mycoplasma / Q000032:analysis* / Q000187:drug effects / Q000378:metabolism; D009177:Mycoplasma pneumoniae / Q000032:analysis; D009179:Mycoplasmatales / Q000032:analysis / Q000187:drug effects / Q000378:metabolism; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism
D000199:Actins; D001426:Bacterial Proteins; D003285:Contractile Proteins; D003572:Cytochalasins; D010445:Peptide Elongation Factors; D010444:Peptide Elongation Factor Tu