HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Puntervoll, P. Articles by Jensen, H. B. Search for Related Content PubMed PubMed Citation Articles by Puntervoll, P. Articles by Jensen, H. B. Agricola Articles by Puntervoll, P. Articles by Jensen, H. B.

Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins

Department of Molecular Biology, University of Bergen, HiB, Thormøhlensgate 55, N-5020 Bergen, Norway¹

Author for correspondence: Pl Puntervoll. Tel: +47 55584500. Fax: +47 55589683. e-mail: pal.puntervoll{at}mbi.uib.no

Native and recombinant FomA proteins were extracted by detergent from the cell envelopes of Fusobacterium nucleatum and Escherichia coli, and purified to near homogeneity by chromatography. Circular dichroism analysis revealed that the FomA protein consists predominantly of ß-sheets, in line with the previously proposed 16-stranded ß-barrel topology model. Results obtained by trypsin treatment of intact cells and cell envelopes of F. nucleatum, and from limited proteolysis of purified FomA protein, indicated that the N-terminal part of the FomA protein is not an integral part of the ß-barrel, but forms a periplasmic domain. Based on these results a new topology model is proposed for the FomA protein, where the C-terminal part forms a 14-stranded ß-barrel separate from the periplasmic N-terminal domain.

Keywords: Fusobacterium nucleatum, porins, outer-membrane proteins, circular dichroism

Abbreviations: CD, circular dichroism; FomA, fusobacterial outer-membrane protein A; OBG, octyl ß-glucopyranoside; OM, outer membrane; OMP, outer-membrane protein

^a Present address: Lehrstuhl für Biotechnologie, Theodor-Boveri-Institut (Biozentrum) der Universität Würzburg, Germany.

This article has been cited by other articles:

				H. Nikaido Molecular Basis of Bacterial Outer Membrane Permeability Revisited Microbiol. Mol. Biol. Rev., December 1, 2003; 67(4): 593 - 656. [Abstract] [Full Text] [PDF]