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

Publication ,  Journal Article
Surana, NK; Grass, S; Hardy, GG; Li, H; Thanassi, DG; Geme, JWS
Published in: Proc Natl Acad Sci U S A
October 5, 2004

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.

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

October 5, 2004

Volume

101

Issue

40

Start / End Page

14497 / 14502

Location

United States

Related Subject Headings

  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Microscopy, Electron
  • Haemophilus influenzae
  • Evolution, Molecular
  • Bacterial Outer Membrane Proteins
 

Citation

APA
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MLA
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Surana, N. K., Grass, S., Hardy, G. G., Li, H., Thanassi, D. G., & Geme, J. W. S. (2004). Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution. Proc Natl Acad Sci U S A, 101(40), 14497–14502. https://doi.org/10.1073/pnas.0404679101
Surana, Neeraj K., Susan Grass, Gail G. Hardy, Huilin Li, David G. Thanassi, and Joseph W St Geme. “Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution.Proc Natl Acad Sci U S A 101, no. 40 (October 5, 2004): 14497–502. https://doi.org/10.1073/pnas.0404679101.
Surana NK, Grass S, Hardy GG, Li H, Thanassi DG, Geme JWS. Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution. Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14497–502.
Surana, Neeraj K., et al. “Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution.Proc Natl Acad Sci U S A, vol. 101, no. 40, Oct. 2004, pp. 14497–502. Pubmed, doi:10.1073/pnas.0404679101.
Surana NK, Grass S, Hardy GG, Li H, Thanassi DG, Geme JWS. Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution. Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14497–14502.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

October 5, 2004

Volume

101

Issue

40

Start / End Page

14497 / 14502

Location

United States

Related Subject Headings

  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Microscopy, Electron
  • Haemophilus influenzae
  • Evolution, Molecular
  • Bacterial Outer Membrane Proteins