The flagellar anti-sigma factor FlgM actively dissociates Salmonella typhimurium sigma28 RNA polymerase holoenzyme

Article Abstract:

The anti-sigma factor of Salmonella typhimurium, FlgM, actively splits its RNA polymerase holoenzyme, sigma28. FlgM holds back transcription of class 3 flagellar genes. It does so through directly interacting with sigma28, the flagellar-specific sigma factor. Probably FlgM stops RNA polymerase (RNAP) holoenzyme formation by holding on to free sigma28. FlgM-mediated inhibition of sigma28 activity in vitro has been analyzed. FlgM can hold back sigma28 activity when sigma28 first is allowed to be close to core RNAP. It seems that a secondary activity of FlgM, which can be called holoenzyme destabilization, adds to the sensitivity of the cell to changes in FlgM levels during flagellar biogenesis.

Analysis, Observations, Bacteria, Genetic regulation, Gene expression, Genetic transcription, Transcription (Genetics), RNA polymerases, Cellular control mechanisms, Cell regulation, Salmonella typhimurium, Nucleic acids, Nucleic acid isolation

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The flagellar-specific transcription factor, [sigma.sup.28], is the Type III secretion chaperone for the flagellar-specific anti-[sigma.sup.28] factor FlgM

Article Abstract:

Isolation of mutant in the flagellar-specific transcription factor [sigma.sup.28] that is specific for FlgM-facilitated secretion is described. The data demonstrate that [sigma.sup.28] is the Type III secretion chaperone for its own anti-sigma factor FlgM.

United States, Gene mutations, Gene mutation, DNA binding proteins, Molecular chaperones

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The mechanism of outer membrane penetration by the eubacterial flagellum and implications for spirochete evolution

Article Abstract:

The paper presents the mutants in the distal rod of flagellum protein and the growth of flagella as in spirochetes. Outer membrane penetration shows efficient coupling.

Cell membranes, Spirochetes, Structure, Report

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