The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

pilQ  -  nucleotide-binding protein

Escherichia coli

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of pilQ

  • DNA sequencing of the region upstream of pilQ revealed the presence of two open reading frames (ORFs) whose deduced polypeptides shared significant identities with proteins required for pilus expression in Pseudomonas aeruginosa and Pseudomonas syringae, the genes for which are arrayed upstream of a gene encoding a PilQ homologue [1].
  • The piliation defects in the mutants could not be ascribed to polarity on distal pilQ expression as shown by direct measurement of PilQ antigen in those backgrounds and the use of a novel technique to create tandem duplications in the gonococcus (Gc) genome [1].
  • PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a high-molecular-mass multimer [1].
 

High impact information on pilQ

  • We identified 38 positive clones in the screen, encoding pili (PilA and TcpA), cell membrane proteins (PilQ, MshO, MshP, and CapK), methyl-accepting chemotaxis proteins, chemotaxis and motility proteins (CheA and CheR), a quorum-sensing protein (LuxP), and four hypothetical proteins [2].
  • These results suggest that PilA and its outer membrane secretin, PilQ, are expressed during human infection and may be involved in colonization of the gastrointestinal tract [2].
  • These results indicate that ATPase activity of the PilQ multimer is essential for R64 thin pilus biogenesis [3].
  • To analyze the relationship between structure and function of PilQ protein, amino acid substitutions were introduced within several conserved motifs [3].
  • Previous studies have shown that products of several ancillary pil genes are required for organelle biogenesis but of these only PilQ, a member of the GspD protein family, is a component of the outer membrane [1].
 

Analytical, diagnostic and therapeutic context of pilQ

  • 5. By gel filtration chromatography, PilQ protein was eluted at the position corresponding to 460 kDa, suggesting that PilQ protein forms a homooctamer [3].

References

  1. PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a high-molecular-mass multimer. Drake, S.L., Sandstedt, S.A., Koomey, M. Mol. Microbiol. (1997) [Pubmed]
  2. Use of in vivo-induced antigen technology (IVIAT) to identify genes uniquely expressed during human infection with Vibrio cholerae. Hang, L., John, M., Asaduzzaman, M., Bridges, E.A., Vanderspurt, C., Kirn, T.J., Taylor, R.K., Hillman, J.D., Progulske-Fox, A., Handfield, M., Ryan, E.T., Calderwood, S.B. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Atpase activity and multimer formation of Pilq protein are required for thin pilus biogenesis in plasmid R64. Sakai, D., Horiuchi, T., Komano, T. J. Biol. Chem. (2001) [Pubmed]
 
WikiGenes - Universities