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A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4641987
Author(s) Nickerson, Nicholas N.; Abby, Sophie S.; Rocha, Eduardo P. C.; Chami, Mohamed; Pugsley, Anthony P.
Author(s) at UniBasel Chami, Mohamed
Year 2012
Title A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin
Journal Journal of Bacteriology
Volume 194
Number 18
Pages / Article-Number 4951-8
Mesh terms Amino Acid Substitution; Bacteria, enzymology; Cluster Analysis; Fimbriae Proteins, genetics, metabolism; Inovirus, enzymology; Liposomes, metabolism; Mutant Proteins, genetics, metabolism; Phylogeny; Protein Multimerization; Secretin, genetics, metabolism; Sequence Homology, Amino Acid
Abstract Secretins form large multimeric complexes in the outer membranes of many Gram-negative bacteria, where they function as dedicated gateways that allow proteins to access the extracellular environment. Despite their overall relatedness, different secretins use different specific and general mechanisms for their targeting, assembly, and membrane insertion. We report that all tested secretins from several type II secretion systems and from the filamentous bacteriophage f1 can spontaneously multimerize and insert into liposomes in an in vitro transcription-translation system. Phylogenetic analyses indicate that these secretins form a group distinct from the secretins of the type IV piliation and type III secretion systems, which do not autoassemble in vitro. A mutation causing a proline-to-leucine substitution allowed PilQ secretins from two different type IV piliation systems to assemble in vitro, albeit with very low efficiency, suggesting that autoassembly is an inherent property of all secretins.
Publisher American Society for Microbiology
ISSN/ISBN 0021-9193 ; 1098-5530
edoc-URL https://edoc.unibas.ch/87964/
Full Text on edoc No
Digital Object Identifier DOI 10.1128/JB.00798-12
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/22773793
ISI-Number WOS:000308446100020
Document type (ISI) Journal Article
 
   

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