HP0958 is an essential motility gene in Helicobacter pylori

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TY  - JOUR
  - Ryan, KA,Karim, N,Worku, M,Moore, SA,Penn, CW,O'Toole, PW
  - 2005
  - May
  - Fems Microbiology Letters
  - HP0958 is an essential motility gene in Helicobacter pylori
  - Validated
  - ()
  - Helicobacter pylori flagella motility transcription GASTRIC EPITHELIAL-CELLS ESCHERICHIA-COLI GNOTOBIOTIC PIGLETS FLAGELLAR EXPORT RNA-POLYMERASE PROTEIN COLONIZATION IDENTIFICATION SALMONELLA VIRULENCE
  - 248
  - 47
  - 55
  - Motility is an essential colonization factor for the human gastric pathogen Helicobacter pylori. The H. pylori genome encodes most known flagellar proteins, although a number of key transcription regulators, chaperones, and structural proteins have not yet been identified. Using recently published yeast two-hybrid data we identified HP0958 as a potential motility-associated protein due to its strong interactions with RpoN (sigma(54)) and FliH, a flagellar ATPase regulator. HP0958 exhibits no sequence similarity to any published flagellar genes but contains a carboxy-terminal zinc finger domain that could function in nucleic acid or protein binding. We created a HP0958 mutant by inserting a chloramphenicol resistance marker into the gene using a PCR-based allelic exchange method and the resultant mutant was non-motile as measured by a BacTracker instrument. Electron microscopic analysis revealed that the HP0958 mutant cells were aflagellate and Western blot analysis revealed a dramatic reduction in flagellin and hook protein production. The HP0958 mutant also showed decreased transcription of flgE,flaB and flaA as well as the checkpoint genes flhA and flhF. Expression of flgM was increased relative to the wild-type and both rpoN and fliA (sigma(28)) expression were unchanged. We conclude that HP0958 is essential for normal motility and flagella production, and represents a novel flagellar component in the epsilon proteobacteria. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
  - DOI 10.1016/j.femsle.2005.05.022
DA  - 2005/05
ER  - 
@article{V43337192,
   = {Ryan,  KA and Karim,  N and Worku,  M and Moore,  SA and Penn,  CW and O'Toole,  PW },
   = {2005},
   = {May},
   = {Fems Microbiology Letters},
   = {HP0958 is an essential motility gene in Helicobacter pylori},
   = {Validated},
   = {()},
   = {Helicobacter pylori flagella motility transcription GASTRIC EPITHELIAL-CELLS ESCHERICHIA-COLI GNOTOBIOTIC PIGLETS FLAGELLAR EXPORT RNA-POLYMERASE PROTEIN COLONIZATION IDENTIFICATION SALMONELLA VIRULENCE},
   = {248},
  pages = {47--55},
   = {{Motility is an essential colonization factor for the human gastric pathogen Helicobacter pylori. The H. pylori genome encodes most known flagellar proteins, although a number of key transcription regulators, chaperones, and structural proteins have not yet been identified. Using recently published yeast two-hybrid data we identified HP0958 as a potential motility-associated protein due to its strong interactions with RpoN (sigma(54)) and FliH, a flagellar ATPase regulator. HP0958 exhibits no sequence similarity to any published flagellar genes but contains a carboxy-terminal zinc finger domain that could function in nucleic acid or protein binding. We created a HP0958 mutant by inserting a chloramphenicol resistance marker into the gene using a PCR-based allelic exchange method and the resultant mutant was non-motile as measured by a BacTracker instrument. Electron microscopic analysis revealed that the HP0958 mutant cells were aflagellate and Western blot analysis revealed a dramatic reduction in flagellin and hook protein production. The HP0958 mutant also showed decreased transcription of flgE,flaB and flaA as well as the checkpoint genes flhA and flhF. Expression of flgM was increased relative to the wild-type and both rpoN and fliA (sigma(28)) expression were unchanged. We conclude that HP0958 is essential for normal motility and flagella production, and represents a novel flagellar component in the epsilon proteobacteria. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.}},
   = {DOI 10.1016/j.femsle.2005.05.022},
  source = {IRIS}
}
AUTHORSRyan, KA,Karim, N,Worku, M,Moore, SA,Penn, CW,O'Toole, PW
YEAR2005
MONTHMay
JOURNAL_CODEFems Microbiology Letters
TITLEHP0958 is an essential motility gene in Helicobacter pylori
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDHelicobacter pylori flagella motility transcription GASTRIC EPITHELIAL-CELLS ESCHERICHIA-COLI GNOTOBIOTIC PIGLETS FLAGELLAR EXPORT RNA-POLYMERASE PROTEIN COLONIZATION IDENTIFICATION SALMONELLA VIRULENCE
VOLUME248
ISSUE
START_PAGE47
END_PAGE55
ABSTRACTMotility is an essential colonization factor for the human gastric pathogen Helicobacter pylori. The H. pylori genome encodes most known flagellar proteins, although a number of key transcription regulators, chaperones, and structural proteins have not yet been identified. Using recently published yeast two-hybrid data we identified HP0958 as a potential motility-associated protein due to its strong interactions with RpoN (sigma(54)) and FliH, a flagellar ATPase regulator. HP0958 exhibits no sequence similarity to any published flagellar genes but contains a carboxy-terminal zinc finger domain that could function in nucleic acid or protein binding. We created a HP0958 mutant by inserting a chloramphenicol resistance marker into the gene using a PCR-based allelic exchange method and the resultant mutant was non-motile as measured by a BacTracker instrument. Electron microscopic analysis revealed that the HP0958 mutant cells were aflagellate and Western blot analysis revealed a dramatic reduction in flagellin and hook protein production. The HP0958 mutant also showed decreased transcription of flgE,flaB and flaA as well as the checkpoint genes flhA and flhF. Expression of flgM was increased relative to the wild-type and both rpoN and fliA (sigma(28)) expression were unchanged. We conclude that HP0958 is essential for normal motility and flagella production, and represents a novel flagellar component in the epsilon proteobacteria. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
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DOI_LINKDOI 10.1016/j.femsle.2005.05.022
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