PMID:11309495
| Citation |
Mori, H and Ito, K (2001) An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY. Proc. Natl. Acad. Sci. U.S.A. 98:5128-33 |
|---|---|
| Abstract |
The SecY/Sec61alpha family of membrane proteins are the central subunits of the putative protein translocation channel. We introduced random mutations into a segment of Escherichia coli SecY within its cytoplasmic domain 5, which was shown previously to be important for the SecA-dependent translocation activity. Mutations were classified into those retaining function and those gaining a dominant-interfering ability caused by a loss of function. These analyses showed that Arg-357, Pro-358, Gly-359, and Thr-362 are functionally important; Arg-357, conserved in almost all organisms, was identified as an indispensable residue. |
| Links |
PubMed PMC33175 Online version:10.1073/pnas.081617398 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Amino Acid Substitution/genetics; Animals; Arginine/genetics; Arginine/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; Conserved Sequence/genetics; Escherichia coli/genetics; Escherichia coli Proteins; Genes, Dominant/genetics; Genetic Complementation Test; Humans; Membrane Transport Proteins; Molecular Sequence Data; Mutation/genetics; Phenotype; Protein Structure, Tertiary; Protein Subunits; Protein Transport; Serine/genetics; Serine/metabolism; Tyrosine/genetics; Tyrosine/metabolism |
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