Purification of an RNA polymerase II transcript release factor from Drosophila.
Factor 2 was previously identified in Drosophila Kc cell nuclear extract (KcN) as an activity suppressing the appearance of long transcripts (Price, D. H., Sluder, A. E., and Greenleaf, A. L. (1987) J. Biol. Chem. 262, 3244-3255). A 154-kDa protein with factor 2 activity was purified to apparent homogeneity from KcN. An immobilized template assay indicated that factor 2 caused the release of transcripts by RNA polymerase II in an ATP-dependent manner. Some early elongation complexes were resistant to factor 2 action but became sensitive after treatment with 1 M KCl. In the absence of factor 2, transcription complexes still exhibited a low degree of processivity suggesting that factor 2 was only partially responsible for abortive elongation.
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Department of Biochemistry, University of Iowa, Iowa City 52242, USA.
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D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D004331:Drosophila melanogaster; D004591:Electrophoresis, Polyacrylamide Gel; D012319:RNA Polymerase II / Q000378:metabolism*; D012265:Ribonucleotides / Q000378:metabolism; D013489:Suppression, Genetic; D014157:Transcription Factors / Q000302:isolation & purification* / Q000378:metabolism*; D014158:Transcription, Genetic
D012265:Ribonucleotides; D014157:Transcription Factors; D012319:RNA Polymerase II; D000251:Adenosine Triphosphatases; C109658:RNA polymerase II transcript release factor 2