Stability of Mycoplasma pneumoniae Cytadherence-Accessory Protein HMW1 Correlates with Its Association with the Triton Shell
نویسندگان
چکیده
منابع مشابه
Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts.
A cell-free system was used to characterize the phosphorylation of Mycoplasma pneumoniae proteins HMW1 and HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infection. The pH and cation requirements for phosphorylation of HMW1 and HMW2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibito...
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The stability of cytadherence proteins in Mycoplasma pneumoniae requires activity of the protein kinase PrkC.
Mycoplasma pneumoniae belongs to the mollicutes, a group of bacteria that have strongly reduced genomes but that are nevertheless capable of independent life. With only three transcription factors, the regulatory features of these bacteria are very limited. Thus, posttranslational regulation might be important for M. pneumoniae. In addition to the highly specific HPr kinase, the M. pneumoniae p...
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15 صفحه اولStability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae.
The surface protein P65 is a constituent of the Mycoplasma pneumoniae cytoskeleton and is present at reduced levels in mutants lacking the cytadherence accessory protein HMW2. Pulse-chase studies demonstrated that P65 is subject to accelerated turnover in the absence of HMW2. P65 was also less abundant in noncytadhering mutants lacking HMW1 or P30 but was present at wild-type levels in mutants ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2001
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.183.12.3680-3688.2001