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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...

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Detalles Bibliográficos
Autor principal: Neimark, H.
Formato: Texto
Lenguaje:English
Publicado: Yale Journal of Biology and Medicine 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2590547/
https://www.ncbi.nlm.nih.gov/pubmed/6433566
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author Neimark, H.
author_facet Neimark, H.
author_sort Neimark, H.
collection PubMed
description 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.
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spelling pubmed-25905472008-11-28 Mycoplasma and bacterial proteins resembling contractile proteins: a review. Neimark, H. Yale J Biol Med Research Article 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. Yale Journal of Biology and Medicine 1983 /pmc/articles/PMC2590547/ /pubmed/6433566 Text en
spellingShingle Research Article
Neimark, H.
Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title_full Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title_fullStr Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title_full_unstemmed Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title_short Mycoplasma and bacterial proteins resembling contractile proteins: a review.
title_sort mycoplasma and bacterial proteins resembling contractile proteins: a review.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2590547/
https://www.ncbi.nlm.nih.gov/pubmed/6433566
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