Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/43759
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Type: Journal article
Title: Genes involved in Sec-independent membrane targeting of hydrogenase in Azotobacter chroococcum
Author: de Souza, E.
Pedrosa, F.
Wassem, R.
Ford, C.
Yates, M.
Citation: Research in Microbiology, 2007; 158(3):272-278
Publisher: Editions Scientifiques Medicales Elsevier
Issue Date: 2007
ISSN: 0923-2508
1769-7123
Statement of
Responsibility: 
Emanuel Maltempi de Souza, Fábio de Oliveira Pedrosa, Roseli Wassem, Chris M. Ford and M. Geoffrey Yates
Abstract: Sec-independent translocation systems have been characterised in Escherichia coli and other bacteria and differ from the Sec-dependent system by transporting fully folded proteins using the transmembrane proton electrochemical gradient. Proteins transported by this system bear a twin-arginine motif (tat) in the N-terminal signal peptide and include several cofactor-containing proteins. Azotobacter chroococcum strain (MCD124) has a soluble hydrogenase, which exhibited low O(2)-dependent H(2) uptake, and a shift in the pH of the culture to a more alkaline range during growth. We show that the DNA region capable of complementing this strain contains the tatABC genes and that mutations in the tatA gene reproduced the soluble hydrogenase and the culture pH shift phenotypes. We also show that insertional mutation in the tatC gene at a position corresponding to its C-terminal region had no effect on hydrogenase activity, but induced the pH shift of the culture. Sequence and mutagenesis analyses of this genomic region suggest that these genes form an operon that does not contain a tatD-like gene. A mutation in hupZ of the main hup gene region, coding for a possible b-type cytochrome also yielded a soluble hydrogenase, but not the pH-shift phenotype.
Keywords: Cell Membrane; Azotobacter; Hydrogenase; Bacterial Proteins; Mutagenesis; Protein Binding; Biological Transport; Phenotype; Mutation; Genes, Bacterial; Hydrogen-Ion Concentration
Description: Copyright © 2007 Elsevier Masson SAS All rights reserved.
RMID: 0020070653
DOI: 10.1016/j.resmic.2007.01.001
Description (link): http://www.elsevier.com/wps/find/journaldescription.cws_home/522493/description#description
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