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Purification and functional characterization of transcription factor SII from calf thymus. Role in RNA polymerase II elongation


Purification and functional characterization of transcription factor SII from calf thymus. Role in RNA polymerase II elongation



Journal of Biological Chemistry 262(11): 5227-5232



ISSN/ISBN: 0021-9258

PMID: 3558392

SII was purified from calf thymus tissue to apparent homogeneity by a rapid procedure. The 38-kDa protein stimulated RNA synthesis by purified calf thymus RNA polymerase II 4-fold. The calf thymus SII had similar chromatographic properties and molecular size and cross-reacted immunologically with antibodies to mouse SII (Sekimizu, K., Nakanishi, Y., Mizuno, D., and Natori, S. (1979) Biochemistry 18, 1582-1588). We have substituted the purified calf thymus SII for the partially purified HeLa transcription factor IIS fraction in a HeLa (human) transcription system reconstituted with purified factors and RNA polymerase II. The purified protein stimulated specific transcription from the adenovirus 2 major late promoter by increasing the efficiency of the elongation reaction.

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Accession: 006228021

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