Translocator proteins in the two-partner secretion family have multiple domains

The Journal of Biological Chemistry
Neeraj K SuranaJ W St Geme

Abstract

The two-partner secretion pathway in Gram-negative bacteria consists of a TpsA exoprotein and a cognate TpsB outer membrane translocator protein. Previous work has demonstrated that the TpsB protein forms a beta-barrel structure with pore forming activity and facilitates translocation of the TpsA protein across the outer membrane. In this study, we characterized the functional domains of the Haemophilus influenzae HMW1B protein, a TpsB protein that interacts with the H. influenzae HMW1 adhesin. Using c-Myc epitope tag insertions and cysteine substitution mutagenesis, we discovered that HMW1B contains an N-terminal surface-localized domain, an internal periplasmic domain, and a C-terminal membrane anchor. Functional and biochemical analysis of the c-Myc epitope tag insertions and a series of HMW1B deletion constructs demonstrated that the periplasmic domain is required for secretion of HMW1 and that the C-terminal membrane anchor (HMW1B-(234-545)) is capable of oligomerization and pore formation. Similar to our observations with HMW1B, examination of a Bordetella pertussis TpsB protein called FhaC revealed that the C terminus of FhaC (FhaC-(232-585)) is capable of pore formation. We speculate that all TpsB proteins have a modula...Continue Reading

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Citations

Apr 12, 2008·The Journal of Biological Chemistry·Guillaume DuretAnne H Delcour
Aug 19, 2007·Journal of Bacteriology·Huilin LiJoseph W St Geme
Apr 12, 2014·PLoS Pathogens·Jessica R McCann, Joseph W St Geme
Aug 8, 2009·Trends in Microbiology·Joseph W St Geme, Hye-Jeong Yeo
Nov 9, 2007·Trends in Microbiology·Joseph Mazar, Peggy A Cotter
Oct 5, 2007·Research in Microbiology·Hélène Hodak, Françoise Jacob-Dubuisson
Nov 26, 2013·Biochimica Et Biophysica Acta·Peter van UlsenJoen Luirink

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