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• W2092374482 startingPage "1750" @default.
• W2092374482 abstract "Mycoplasma pneumoniae exhibits a novel form of gliding motility that is mediated by the terminal organelle, a differentiated polar structure. Given that genes known to be involved in gliding in other organisms are absent in M. pneumoniae, random transposon mutagenesis was employed to generate mutants with gliding-deficient phenotypes. Transposon insertions in the only annotated Ser/Thr protein kinase gene (prkC; MPN248) and its cognate phosphatase gene (prpC; MPN247) in M. pneumoniae resulted in significant and contrasting effects on gliding frequencies. prkC mutant cells glided at approximately half the frequency of wild-type cells, while prpC mutant cells glided more than twice as frequently as wild-type cells. Phosphoprotein staining confirmed the association between phosphorylation of the cytoskeletal proteins HMW1 and HMW2 and membrane protein P1 and the gliding phenotype. When the prpC mutant was complemented by transposon delivery of a wild-type copy of the prpC allele, gliding frequencies and phosphorylation levels returned to the wild-type standard. Surprisingly, delivery of the recombinant wild-type prkC allele dramatically increased gliding frequency to a level approximately 3-fold greater than that of wild-type in the prkC mutant. Collectively, these data suggest that PrkC and PrpC work in opposition in M. pneumoniae to influence gliding frequency." @default.
• W2092374482 created "2016-06-24" @default.
• W2092374482 creator A5010139321 @default.
• W2092374482 creator A5070505260 @default.
• W2092374482 date "2013-04-15" @default.
• W2092374482 modified "2023-09-25" @default.
• W2092374482 title "Protein Kinase/Phosphatase Function Correlates with Gliding Motility in Mycoplasma pneumoniae" @default.
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• W2092374482 doi "https://doi.org/10.1128/jb.02277-12" @default.
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