Linked Life Data

8899718

Source:http://linkedlifedata.com/resource/pubmed/id/8899718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-19
pubmed:databankReference
pubmed:abstractText
Type 4 fimbriae of Pseudomonas aeruginosa are surface filaments involved in host colonization. They mediate both attachment to host epithelial cells and flagelia-independent twitching motility. Four additional genes, pilW, pilX, pilY1 and pilY2, are located on Spel fragment E in the 5 kb intergenic region between the previously characterized genes pilV and pilE, which encode prepilin-like proteins involved in type 4 fimbrial biogenesis. The phenotypes of a transposon insertion and other mutations constructed by allelic exchange show that these genes are involved in the assembly of type 4 fimbriae. The PilW and PilX proteins are membrane located, possess the hydrophobic N-terminus characteristic of prepilin-like proteins, and appear to belong to the GspJ and GspK group of proteins that are required for protein secretion in a wide range of Gram-negative bacteria. These findings increase the similarities between the fimbrial biogenesis and the Gsp-based protein-secretion supersystems. PilY1 is a large protein with C-terminal homology to the PilC2 protein of Neisseria gonorrhoeae, thought to be a fimbrial tip-associated adhesin, and which, like PilY1, is involved in fimbrial assembly. PilY1 appears to be located in both the membrane and the external fimbrial fractions. PilY2 is a small protein that appears to play a subtle role in fimbrial biogenesis and represents a new class of protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8899718-Alleles, pubmed-meshheading:8899718-Amino Acid Sequence, pubmed-meshheading:8899718-Bacterial Proteins, pubmed-meshheading:8899718-DNA, Bacterial, pubmed-meshheading:8899718-Fimbriae, Bacterial, pubmed-meshheading:8899718-Fimbriae Proteins, pubmed-meshheading:8899718-Gene Expression, pubmed-meshheading:8899718-Genes, Bacterial, pubmed-meshheading:8899718-Genetic Complementation Test, pubmed-meshheading:8899718-Membrane Proteins, pubmed-meshheading:8899718-Molecular Sequence Data, pubmed-meshheading:8899718-Mutagenesis, Insertional, pubmed-meshheading:8899718-Mutation, pubmed-meshheading:8899718-Neisseria gonorrhoeae, pubmed-meshheading:8899718-Open Reading Frames, pubmed-meshheading:8899718-Phenotype, pubmed-meshheading:8899718-Pseudomonas aeruginosa, pubmed-meshheading:8899718-Sequence Analysis, DNA, pubmed-meshheading:8899718-Sequence Homology, Amino Acid
pubmed:year
1996
pubmed:articleTitle
Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pilY1 encodes a gonococcal PilC homologue.
pubmed:affiliation
Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't