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Identification of a component separated on Mono Q purification of Escherichia coli RNA polymerase as an NTPase
Author(s) -
Butzow James J.,
Stankis Rosemary G.
Publication year - 1992
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(92)80166-e
Subject(s) - escherichia coli , rna polymerase , chemistry , protein subunit , biochemistry , gel electrophoresis , polymerase , enterobacteriaceae , rna , enzyme , microbiology and biotechnology , chromatography , biology , gene
Standard preparations of Escherichia coli RNA polymerase (RNAP) contain NTPase activity. High‐performance anion exchange chromatography on Mono Q has recently been used by Hager et al. [1990, Biochemistry 29, 7890–7894] to fractionate RNAP into holoenzyme (α,ββ′σ) and core (α,ββ′) forms, plus other protein components. We found that one of these components, of protomer size slightly larger than the σ 70 subunit, has NTPase activity; it is efficiently separated on Mono Q, leaving transcriptionally active holoenzyme and core apparently free of NTPase activity. Because of the similarity in size with σ 70 , the NTPase component may escape detection by routine gel electrophoresis.