The rapid degradation of mutant secA protein in the Bacillus subtilis secA341 (ts) mutant causes a protein translocation defect in the cell
To study the function of SecA protein and the protein translocation system of Bacillus subtilis, wild-type and mutant SecA proteins were characterized in vivo and in vitro. SecA protein was abundant in a wild-type strain (168) and existed in a stable homodimer. In contrast to this, SecA341 (ts) prot...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 58; no. 10; pp. 1845 - 1850 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Japan Society for Bioscience Biotechnology and Agrochemistry
01.10.1994
Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | To study the function of SecA protein and the protein translocation system of Bacillus subtilis, wild-type and mutant SecA proteins were characterized in vivo and in vitro. SecA protein was abundant in a wild-type strain (168) and existed in a stable homodimer. In contrast to this, SecA341 (ts) protein having an amino acid replacement from proline to leucine at residue 431 was undetectable by immunoblotting in the cell lysate of a secA341 mutant (TB301) at the nonpermissive temperature, 42 degrees C. Pulse-chase studies using 35S-methionine showed that newly synthesized SecA protein was rapidly degraded in the mutant at 42 degrees C. Purified SecA341 protein was more sensitive to trypsin and subtilisin than purified wild-type SecA protein in the presence of ATP. These results indicate that the secA341 mutation causes the rapid degradation of mutant SecA protein and a concomitant protein translocation defect in the cell. |
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Bibliography: | F30 9501534 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.58.1845 |