Heat shock caused a more active formation of the "dormant" forms (minibodies), as well as increased production of extracellular membrane vesicles by Acholeplasma laidlawii PG-8A cells. Raise of the amount of the minibodies that have increased resistance to biogenic and abiogenic stress factors and pathogenicity may lead to more successful persistence of mycoplasmas in their hosts. Increased production of the extracellular membrane vesicles containing virulence factors by Acholeplasma laidlawii cells during stress may be an additional burden for the infected organism.
View Article and Find Full Text PDFMycoplasmas (class Mollicutes) are the most simply organized prokaryotic organisms capable to self-reproduction. They are considered as a model of "minimal" cell. Systems preserved by mycoplasmas in their reductive evolution may play a fundamental role in viability of any cell.
View Article and Find Full Text PDFLocalization of the protein FtsZ in Mycoplasma hominis cells was determined. Ultra thin sections were treated by rabbit polyclonal antibodies against FtsZ M. hominis: a conjugate of protein A with colloidal gold particles was used instead of secondary antibodies.
View Article and Find Full Text PDFA considerable increase in several heat shock proteins (HSPs) amount in Acholeplasma laidlawii cells has been revealed after temperature rising of liquid culture; and the quantity of small HSP, named p17, was increased in a hundred of times. The p17 protein was isolated and identified as HSP of alpha-crystallin type (alpha-HSP). It became possible as a result of sequencing of 15 amino acids from N-terminal of the p17 polypeptide chain, followed by revealing of a corresponding open reading frame (ORF) in a completely sequenced genome of A.
View Article and Find Full Text PDFIn this review we have tried to describe proteins and supermolecular structures which take part in the division of bacterial cell. The principal cell division protein of the most of prokaryotes is FtsZ, a homologue of eukaryotic tubulin. FtsZ just as tubulin is capable to bind and hydrolyze GTP.
View Article and Find Full Text PDF