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© Research
Publication : Journal of bacteriology

A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of bacteriology - 06 Jul 2012

Nickerson NN, Abby SS, Rocha EP, Chami M, Pugsley AP

Link to Pubmed [PMID] – 22773793

J. Bacteriol. 2012 Sep;194(18):4951-8

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.

http://www.ncbi.nlm.nih.gov/pubmed/22773793