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PURIFICATION AND PROPERTIES OF SACCHAROMYCES-CEREVISIAE RNA POLYMERASE-II GENERAL INITIATION FACTOR-A
Author(s): SAYRE MH, TSCHOCHNER H, KORNBERG RD
Source: JOURNAL OF BIOLOGICAL CHEMISTRY    Volume: 267    Issue: 32    Pages: 23383-23387    Published: NOV 15 1992  
Times Cited: 40     References: 27     
Abstract: RNA polymerase II initiation factor a was purified to apparent homogeneity from yeast whole cell extract and consisted of two highly charged polypeptides with apparent masses of 66 and 43 kDa. Separation and renaturation of the subunits showed that both were required for transcription activity. The native mass of factor a was estimated to be 240-260 kDa by gel filtration, but its sedimentation rate in a glycerol gradient was similar to that of a much smaller globular protein, suggesting an extended conformation. Factor a was required for utilization of six different eukaryotic promoters in vitro, indicating a general role in promoter-directed transcription by yeast RNA polymerase II.
Document Type: Article
Language: English
Reprint Address: SAYRE, MH (reprint author), STANFORD UNIV, MED CTR, SCH MED, DEPT CELL BIOL, STANFORD, CA 94305 USA
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814
Subject Category: Biochemistry & Molecular Biology
IDS Number: JY163
ISSN: 0021-9258
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