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MULTIFUNCTIONAL RNA POLYMERASE-II INITIATION FACTOR-DELTA FROM RAT-LIVER - RELATIONSHIP BETWEEN CARBOXYL-TERMINAL DOMAIN KINASE, ATPASE, AND DNA HELICASE ACTIVITIES
Author(s): SERIZAWA H, CONAWAY RC, CONAWAY JW
Source: JOURNAL OF BIOLOGICAL CHEMISTRY    Volume: 268    Issue: 23    Pages: 17300-17308    Published: AUG 15 1993  
Times Cited: 59     References: 61     
Abstract: RNA polymerase II initiation factor delta was previously purified from rat liver and found to possess a closely associated DNA-dependent ATPase activity and a protein kinase activity capable of phosphorylating the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (Serizawa, H., Conaway, R. C., and Conaway, J. W. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 7476-7480). In addition, delta's human homolog, BTF2(TFIIH), was recently shown to have an associated DNA helicase activity (Schaeffer, L., Roy, R., Humbert, S., Moncollin, V., Vermeulen, W., Hoeijmakers, J. H. J., Chambon, P., and Egly, J.-M. (1993) Science 259, 58-63). Here we demonstrate that initiation factor delta also possesses DNA helicase activity. In addition, we compare the properties of delta's associated CTD kinase, ATPase, and DNA helicase activities. Whereas the enzymatic properties of ATPase and DNA helicase are similar and consistent with the possibility that they could function in ATP-dependent activation of the preinitiation complex, ATPase and CTD kinase exhibit significant differences in their nucleotide specificities, responses to DNA effectors, and sensitivities to inhibitors.
Document Type: Article
Language: English
Reprint Address: SERIZAWA, H (reprint author), OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814
Subject Category: Biochemistry & Molecular Biology
IDS Number: LQ988
ISSN: 0021-9258
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