Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations in the fifth-position glutamate in Pseudomonas aeruginosa pilin affect the transmethylation of the N-terminal phenylalanine.

Canadian journal of microbiology - 1 May 1993

Macdonald D L, Pasloske B L, Paranchych W

Abstract excerpt

The pili of Pseudomonas aeruginosa are composed of 15-kDa pilin monomers that are synthesized in the cytoplasm and assembled in the membrane. Processing occurs between the synthesis and assembly steps. The propilin is cleaved by a unique leader peptidase encoded by pilD, which is adjacent to the pilin structural gene pilA. This generates an N-terminal phenylalanine that is subsequently methylated by an as yet...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Outer Membrane Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Base Sequence

Share to DNA Mutational Analysis

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 8330261
DOI: 10.1139/m93-071

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the fifth-position glutamate in Pseudomonas aeruginosa pilin affect the transmethylation of the N-terminal phenylalanine.PMID 8330261Read ↗

Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review.Semantic proximity Read ↗

Kinetics and sequence specificity of processing of prepilin by PilD, the type IV leader peptidase of Pseudomonas aeruginosa.Semantic proximity Read ↗

Analysis of the pilU gene for the prepilin peptidase involved in the biogenesis of type IV pili encoded by plasmid R64.Semantic proximity Read ↗

Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili.Semantic proximity Read ↗

The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.Semantic proximity Read ↗

Identification of two genes with prepilin-like leader sequences involved in type 4 fimbrial biogenesis in Pseudomonas aeruginosa.Semantic proximity Read ↗

Cloning of an Aeromonas hydrophila type IV pilus biogenesis gene cluster: complementation of pilus assembly functions and characterization of a type IV leader peptidase/N-methyltransferase required for extracellular protein secretion.Semantic proximity Read ↗

Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility.Semantic proximity Read ↗

Multiple roles of the pilus biogenesis protein pilD: involvement of pilD in excretion of enzymes from Pseudomonas aeruginosa.Semantic proximity Read ↗

Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase.Semantic proximity Read ↗

Localization of a critical interface for helical rod formation of bacterial adhesion P-pili.Semantic proximity Read ↗

Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae: critical role of Gly-1 in assembly.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.