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Identification of proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit

by: Rei Ueshima, Nobuyuki Fujita, Akira Ishihama
Biochemical and Biophysical Research Communications, Vol. 184, No. 2. (30 April 1992), pp. 634-639.


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Antisera against a synthetic tetradecameric peptide with the sequence DLIQEGNIGLMKAV, which is present in region 2.2 of both [sigma]70 and [sigma]32 subunits of RNA polymerase, cross-reacted with more than 10 proteins including these two [sigma] subunits. Four major species of these cross-reacting proteins (SCRPs) were purified. N-Terminal amino acid sequence analysis revealed that one of them (SCRP-27A) was an as yet unidentified protein while the other three (SCRP-34, SCRP-27B and SCRP-23) were thioredoxin reductase, ribosomal protein S2, and alkyl hydroperoxide reductase, respectively. Immunological competition experiments with various fragments of this [sigma] region 2.2 peptide indicated that the anti-[sigma] peptide serum contained at least three different species of antibodies. All the four SCRPs analyzed here reacted with an antibody against a C-terminus-proximal epitope.


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