In:
Microbiology, Microbiology Society, Vol. 151, No. 7 ( 2005-07-01), p. 2429-2438
Abstract:
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 PorH C.call and PorH C.eff . Electrophysiological studies of the channels suggested that they are wide and water-filled. Channels formed by PorH C.call are cation-selective, whereas PorH C.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 PorH C.eff . PorH C.call shows high homology to PorH C.eff . PorH C.eff is encoded in the bacterial chromosome by a gene that is localized within the vicinity of the porA gene of C. efficiens . PorH C.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.
Type of Medium:
Online Resource
ISSN:
1350-0872
,
1465-2080
DOI:
10.1099/mic.0.27903-0
Language:
English
Publisher:
Microbiology Society
Publication Date:
2005
detail.hit.zdb_id:
2008736-6
detail.hit.zdb_id:
1180712-X
SSG:
12
Permalink