Overlapping functions of components of a bacterial Sec-independent protein export pathway

被引:440
作者
Sargent, F
Bogsch, EG
Stanley, NR
Wexler, M
Robinson, C
Berks, BC
Palmer, T [1 ]
机构
[1] John Innes Ctr Plant Sci Res, Nitrogen Fixat Lab, Norwich NR4 7UH, Norfolk, England
[2] Univ E Anglia, Sch Biol Sci, Ctr Metalloprot Spect & Biol, Norwich NR4 7TJ, Norfolk, England
[3] Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England
关键词
hydrogenases; molybdoenzymes; periplasm; Sec-independent protein export; twin arginine transfer peptide;
D O I
10.1093/emboj/17.13.3640
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We describe the identification of two Escherichia coli genes required for the export of cofactor-containing periplasmic proteins, synthesized with signal peptides containing a twin arginine motif, Both gene products are homologous to the maize HCF106 protein required for the translocation of a subset of lumenal proteins across the thylakoid membrane. Disruption of either gene affects the export of a range of such proteins, and a complete block is observed when both genes are inactivated. The Sec protein export pathway was unaffected, indicating the involvement of the gene products in a novel export system. The accumulation of active cofactor-containing proteins in the cytoplasm of the mutant strains suggests a role for the gene products in the translocation of folded proteins. One of the two HCF106 homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE, A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the tatB gene.
引用
收藏
页码:3640 / 3650
页数:11
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