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Author

Min, Kyung-Tai
Molecular & Cellular Neurobiology Lab(Min Lab)
Research Interests
  • Local protein synthesis, learning & memory, behavior, mitochondrial dynamics

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ACTIVITY OF MUTANT SIGMA-F PROTEINS TRUNCATED NEAR THE C-TERMINUS

Cited 2 times inthomson ciCited 1 times inthomson ci
Title
ACTIVITY OF MUTANT SIGMA-F PROTEINS TRUNCATED NEAR THE C-TERMINUS
Author
Min, Kyung-TaiYudkin, M.D.
Keywords
BACILLUS-SUBTILIS; RNA-POLYMERASE; LAMBDA-REPRESSOR; DNA; MUTATIONS; SELECTION; SUBUNIT; RECOGNITION; EXPRESSION; CLONING
Issue Date
199211
Publisher
AMER SOC MICROBIOLOGY
Citation
JOURNAL OF BACTERIOLOGY, v.174, no.22, pp.7144 - 7148
Abstract
σ(F), the product of the spoIIAC gene of Bacillus subtilis, is homologous in amino acid sequence throughout most of its length with several other sigma factors of B. subtilis and Escherichia coli. However, 8 residues from the C terminus the homology abruptly breaks down, suggesting that the C-terminal tail of the protein may be dispensable. It is known that an amber mutation at the 11th codon (wild-type glutamine 245) from the C terminus abolishes the function of the sigma factor. We have now placed chain-terminating codons at the ninth codon (wild-type lysine 247), the eighth codon (wild-type valine 248), or the seventh codon (wild-type glutamine 249) from the C terminus. We have tested the resulting mutants for their capacity to sporulate and for their ability to transcribe from a promoter (spoIIIG) that is normally read by RNA polymerase bound to σ(F) (Eσ(F)). The results indicate that a mutant σ(F) lacking the terminal 7 residues functions almost normally, which suggests that glutamine 249 is dispensable. By contrast, lysine 247 is crucial for the activity of σ(F): deletion of the 9 C-terminal residues totally inactivates the protein. When the terminal 8 residues were deleted, placing lysine 247 at the C terminus, the transcriptional activity of the factor is reduced by about 80%: we attribute this effect to neutralization of the positive charge of lysine 247 by formation of a salt bridge with the - COO- terminus.
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ISSN
0021-9193
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