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Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.

Abstract:

The cytoplasmic membrane protein TatB is an essential component of the Escherichia coli twin-arginine (Tat) protein translocation pathway. Together with the TatC component it forms a complex that functions as a membrane receptor for substrate proteins. Structural predictions suggest that TatB is anchored to the membrane via an N-terminal transmembrane alpha-helix that precedes an amphipathic alpha-helical section of the protein. From truncation analysis it is known that both these regions of ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m607295200

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Journal:
Journal of biological chemistry
Volume:
281
Issue:
45
Pages:
34072-34085
Publication date:
2006-11-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
100102

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