Assembly of the Type II Secretion System such as Found in Vibrio cholerae Depends on the Novel Pilotin AspS

• DOI: 10.1371/journal.ppat.1003117
• Publication Date: 2013-01-10T21:53:33Z
• Authors: Rhys A. Dunstan; Eva Heinz; Lakshmi C. Wijeye...; Robert N. Pike; Anthony W. Purcell; Timothy J. Evans; Judyta Praszkier; Roy M. Robins-Browne; Richard A. Strugnell; Konstantin V. Kor...; Trevor Lithgow
• Keywords: Secretin

The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across bacterial outer membrane. A key element in machinery secretin: an integral, multimeric membrane forms pore. We show three distinct T2SSs can be distinguished based on sequence characteristics their secretin pores. Detailed comparative analysis two these, Klebsiella-type and Vibrio-type, showed them to further by pilotin mediates transport assembly into have determined crystal structure novel AspS from Vibrio cholerae, demonstrating convergent evolution wherein functionally equivalent yet structurally unrelated pilotins found Klebsiella other bacteria. binds specific targeting Vibrio-type secretins, enhances kinetics assembly, homologs are all species as well those few strains Escherichia Shigella acquired T2SS.