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

Abstract

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.