Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution.

Published

Journal Article

Omp85-like proteins represent a family of proteins involved in protein translocation, and they are present in all domains of life, except archaea. In eukaryotes, Omp85-like proteins have been demonstrated to form tetrameric pore-forming complexes that interact directly with their substrate proteins. Studies performed with bacterial Omp85-like proteins have demonstrated pore-forming activity but no evidence of multimerization. In this article, we characterize the Haemophilus influenzae HMW1B protein, an Omp85-like protein that has been demonstrated to be critical for secretion of the H. influenzae HMW1 adhesin. Analysis of purified protein by biochemical and electron microscopic techniques revealed that HMW1B forms a tetramer. Examination using liposome-swelling assays demonstrated that HMW1B has pore-forming activity, with a pore size of approximately equal to 2.7 nm. Far-Western blot analysis established that HMW1B interacts with the N terminus of HMW1. These results provide evidence that a bacterial Omp85-like protein forms a tetramer and interacts directly with a substrate protein, suggesting that the architecture and physical properties of Omp85-like proteins have been conserved throughout evolution.

Full Text

Duke Authors

Cited Authors

  • Surana, NK; Grass, S; Hardy, GG; Li, H; Thanassi, DG; Geme, JWS

Published Date

  • October 5, 2004

Published In

Volume / Issue

  • 101 / 40

Start / End Page

  • 14497 - 14502

PubMed ID

  • 15381771

Pubmed Central ID

  • 15381771

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0404679101

Language

  • eng

Conference Location

  • United States