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

1996 ◽  
Vol 19 (4) ◽  
pp. 857-869 ◽  
Author(s):  
Cynthia M. Pepe ◽  
Melvin W. Eklund ◽  
Mark S. Strom
Keyword(s):  
Gene Cluster ◽  
Protein Secretion ◽  
Aeromonas Hydrophila ◽  
Extracellular Protein ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
Leader Peptidase ◽  
Pilus Assembly

Identification and initial characterization of a new pair of sibling sRNAs of Neisseria gonorrhoeae involved in type IV pilus biogenesis

Microbiology ◽  
2021 ◽  
Vol 167 (9) ◽  
Author(s):  
Marie Zachary ◽  
Susanne Bauer ◽  
Maximilian Klepsch ◽  
Katharina Wagler ◽  
Bruno Hüttel ◽  
...  
Keyword(s):  
Target Genes ◽  
Target Prediction ◽  
Type Iv Pilus ◽  
Content Type ◽  
Type Iv ◽  
Gene Expression Control ◽  
Initial Characterization ◽  
Pilus Biogenesis ◽  
Regulatory Rnas

Non-coding regulatory RNAs mediate post-transcriptional gene expression control by a variety of mechanisms relying mostly on base-pairing interactions with a target mRNA. Though a plethora of putative non-coding regulatory RNAs have been identified by global transcriptome analysis, knowledge about riboregulation in the pathogenic Neisseriae is still limited. Here we report the initial characterization of a pair of sRNAs of N. gonorrhoeae , TfpR1 and TfpR2, which exhibit a similar secondary structure and identical single-stranded seed regions, and therefore might be considered as sibling sRNAs. By combination of in silico target prediction and sRNA pulse expression followed by differential RNA sequencing we identified target genes of TfpR1 which are involved in type IV pilus biogenesis and DNA damage repair. We provide evidence that members of the TfpR1 regulon can also be targeted by the sibling TfpR2.

scholarly journals Linkage of the Horizontally Acquired ypm and pil Genes in Yersinia pseudotuberculosis

2005 ◽  
Vol 73 (4) ◽  
pp. 2556-2558 ◽  
Author(s):  
François Collyn ◽  
Hiroshi Fukushima ◽  
Christophe Carnoy ◽  
Michel Simonet ◽  
Pascal Vincent
Keyword(s):  
Gene Cluster ◽  
Yersinia Pseudotuberculosis ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
Pcr Assays

ABSTRACT The superantigen-encoding ypm gene and the pil gene cluster governing type IV pilus biogenesis have been laterally acquired by Yersinia pseudotuberculosis. PCR assays on 270 unrelated strains from various environmental and animal sources revealed a significant association of ypm and pil in isolates.

scholarly journals Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function

2004 ◽  
Vol 55 (1) ◽  
pp. 54-64 ◽  
Author(s):  
Etienne Carbonnelle ◽  
Sophie Hélaine ◽  
Laure Prouvensier ◽  
Xavier Nassif ◽  
Vladimir Pelicic
Keyword(s):  
Neisseria Meningitidis ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
And Function ◽  
Pilus Assembly

scholarly journals Molecular analysis of VcfQ protein involved in Vibrio cholerae type IV pilus biogenesis

2003 ◽  
Vol 52 (4) ◽  
pp. 283-288 ◽  
Author(s):  
Tomoko Miyazato ◽  
Claudia Toma ◽  
Noboru Nakasone ◽  
Koichiro Yamamoto ◽  
Masaaki Iwanaga
Keyword(s):  
Vibrio Cholerae ◽  
Gene Cluster ◽  
Mutational Analysis ◽  
Cell Fractionation ◽  
Deficient Mutant ◽  
Type Iv Pilus ◽  
Outer Membranes ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
Immunological Cross Reaction

The nucleotide sequence of an ORF (vcfQ) within the type IV pilus gene cluster of Vibrio cholerae O34 strain NAGV14 was determined, thereby completing the sequence analysis of the structural operon. The vcfQ gene showed homology to the mshQ gene of the mannose-sensitive haemagglutinin pilus gene cluster. The vcfQ was 651 bp larger than mshQ, and the G+C content of the extra 651 bp portion (35.6 mol%) was lower than that of the overall vcfQ gene (42.5 mol%). Except for the first 270 aa residues, the deduced amino acid sequence of VcfQ showed high homology to the MshQ protein. There was immunological cross-reaction between VcfQ and MshQ by Western blotting. Cell fractionation studies showed that VcfQ is located in both the inner and the outer membranes. Mutational analysis showed that vcfQ-deficient mutant expressed detectable levels of major pilin (VcfA), but failed to assemble them into pili, indicating that VcfQ is essential for pilus assembly. Colony-blotting analyses showed that the N-terminal region of vcfQ is variable in V. cholerae strains.

scholarly journals Type IV Pilus Assembly Proficiency and Dynamics Influence Pilin Subunit Phospho-Form Macro- and Microheterogeneity in Neisseria gonorrhoeae

PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e96419 ◽  
Author(s):  
Åshild Vik ◽  
Jan Haug Anonsen ◽  
Finn Erik Aas ◽  
Finn Terje Hegge ◽  
Norbert Roos ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilin Subunit ◽  
Pilus Assembly

scholarly journals Purification and Three-Dimensional Electron Microscopy Structure of the Neisseria meningitidis Type IV Pilus Biogenesis Protein PilG

2007 ◽  
Vol 189 (17) ◽  
pp. 6389-6396 ◽  
Author(s):  
Richard F. Collins ◽  
Muhammad Saleem ◽  
Jeremy P. Derrick
Keyword(s):  
Electron Microscopy ◽  
Neisseria Meningitidis ◽  
Metal Ion ◽  
Polyacrylamide Gel Electrophoresis ◽  
Three Dimensional ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilus Biogenesis

ABSTRACT Type IV pili are surface-exposed retractable fibers which play a key role in the pathogenesis of Neisseria meningitidis and other gram-negative pathogens. PilG is an integral inner membrane protein and a component of the type IV pilus biogenesis system. It is related by sequence to the extensive GspF family of secretory proteins, which are involved in type II secretion processes. PilG was overexpressed and purified from Escherichia coli membranes by detergent extraction and metal ion affinity chromatography. Analysis of the purified protein by perfluoro-octanoic acid polyacrylamide gel electrophoresis showed that PilG formed dimers and tetramers. A three-dimensional (3-D) electron microscopy structure of the PilG multimer was determined using single-particle averaging applied to samples visualized by negative staining. Symmetry analysis of the unsymmetrized 3-D volume provided further evidence that the PilG multimer is a tetramer. The reconstruction also revealed an asymmetric bilobed structure approximately 125 Å in length and 80 Å in width. The larger lobe within the structure was identified as the N terminus by location of Ni-nitrilotriacetic acid nanogold particles to the N-terminal polyhistidine tag. We propose that the smaller lobe corresponds to the periplasmic domain of the protein, with the narrower “waist” region being the transmembrane section. This constitutes the first report of a 3-D structure of a member of the GspF family and suggests a physical basis for the role of the protein in linking cytoplasmic and periplasmic protein components of the type II secretion and type IV pilus biogenesis systems.

Sign in / Sign up

Export Citation Format

Share Document