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Two functional domains conserved in major and alternate bacterial sigma factors
Author(s) -
Stragier Patrick,
Parsot Claude,
Bouvier Jean
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81203-5
Subject(s) - sigma factor , sigma , chemistry , computational biology , biology , physics , biochemistry , escherichia coli , gene , rna polymerase , quantum mechanics
Sequences of the sigma factors of Escherichia coli and Bacillus subtilis were aligned with the sequences of two sigma‐like proteins, HtpR, involved in the expression of heat‐shock genes in E . coli , and SpoIIG, necessary for endospore formation in B. subtilis . An internal region is highly conserved in the four proteins and is proposed to be involved in binding of sigma factors to core RNA polymerase. The carboxy‐terminal part of the four proteins presents the characteristic structure found in several prokaryotic DNA‐binding proteins and is proposed to be involved in promoter recognition.