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

Nickerson, Nicholas N. and Abby, Sophie S. and Rocha, Eduardo P. C. and Chami, Mohamed and Pugsley, Anthony P.. (2012) A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin. Journal of Bacteriology, 194 (18). pp. 4951-4958.

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Official URL: https://edoc.unibas.ch/87964/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Microbiology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Mar 2022 11:44
Deposited On:08 Mar 2022 11:44

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