Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 151 (2005), 2429-2438; DOI  10.1099/mic.0.27903-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hünten, P.
Right arrow Articles by Benz, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hünten, P.
Right arrow Articles by Benz, R.
Agricola
Right arrow Articles by Hünten, P.
Right arrow Articles by Benz, R.
Microbiology 151 (2005), 2429-2438; DOI  10.1099/mic.0.27903-0
© 2005 Society for General Microbiology

PorH, a new channel-forming protein present in the cell wall of Corynebacterium efficiens and Corynebacterium callunae

Peter Hünten1, Bettina Schiffler1, Friedrich Lottspeich2 and Roland Benz1

1 Lehrstuhl für Biotechnologie, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany
2 Max-Planck-Institute for Biochemistry, Department for Protein Analytics, Am Klopferspitz 18A, D-82152 Martinsried, Germany

Correspondence
Roland Benz
roland.benz{at}mail.uni-wuerzburg.de

Corynebacterium callunae and Corynebacterium efficiens are close relatives of the glutamate-producing mycolata species Corynebacterium glutamicum. The properties of the pore-forming proteins, extracted by organic solvents, were studied. The cell extracts contained channel-forming proteins that formed ion-permeable channels with a single-channel conductance of about 2 to 3 nS in 1 M KCl in a lipid bilayer assay. The corresponding proteins from both corynebacteria were purified to homogeneity and were named PorHC.call and PorHC.eff. Electrophysiological studies of the channels suggested that they are wide and water-filled. Channels formed by PorHC.call are cation-selective, whereas PorHC.eff forms slightly anion-selective channels. Both proteins were partially sequenced. A multiple sequence alignment search within the known chromosome of C. efficiens demonstrated that it contains a gene that fits the partial amino acid sequence of PorHC.eff. PorHC.call shows high homology to PorHC.eff. PorHC.eff is encoded in the bacterial chromosome by a gene that is localized within the vicinity of the porA gene of C. efficiens. PorHC.eff has no signal sequence at the N terminus, which means that it is not exported by the Sec-secretion pathway. The structure of PorH in the cell wall of the corynebacteria is discussed.

Abbreviations: LDAO, N,N-dimethyldodecylamine-N-oxide; PC, diphytanoyl phosphatidylcholine

The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are AJ871585 and AJ871586.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2005 Society for General Microbiology.