Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

BTF2/TFIIH from human, delta from rat, and factor b from yeast are multisubunit basal transcription factors that have been shown to be closely associated with a protein kinase capable of phosphorylating the carboxyl-terminal domain of the large subunit of RNA polymerase II (Lu, H., Zawel, L., Fischer, L., Egly, J. M., and Reinberg, D. (1992) Nature 358, 641-645; Serizawa, H., Conaway, R. C., and Conaway, J. W. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 7476-7480; Feaver, W. J., Gileadi, O., and Kornberg, R. D. (1991) Cell 67, 1223-1230). We report here that a DNA-dependent ATPase and the previously characterized helicase (Schaeffer, L., Roy, R., Humbert, S., Moncollin, V., Vermeulen, W., Hoeijmakers, J., Chambon, P., and Egly, J. M. (1993) Science 260, 58-63) are both associated with BTF2 and reside with the p89 polypeptide subunit. The DNA requirement, the effect of Sarkosyl and staurosporine inhibitors, as well as nucleotide competition experiments, clearly distinguished ATPase/helicase from the carboxyl-terminal domain kinase. Using recombinant wild type or mutated p89/ERCC3 polypeptides and different forms of DNA template, we show the connection between ATPase and the helicase.
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PMID:The DNA-dependent ATPase activity associated with the class II basic transcription factor BTF2/TFIIH. 751 95

The human ERCC3 gene, which corrects specifically the nucleotide excision repair defect in human xeroderma pigmentosum group B and cross-complements the repair deficiency in rodent UV-sensitive mutants of group 3, encodes a presumed DNA helicase that is identical to the p89 subunit of the general transcription factor TFIIH/BTF2. To examine the significance of the postulated functional domains in ERCC3, we have introduced mutations in the ERCC3 cDNA by means of site-specific mutagenesis and have determined the repair capacity of each mutant to complement the UV-sensitive phenotype of rodent group 3 cells. A conservative substitution of arginine for the invariant lysine residue in the ATPase motif (helicase domain I), six deletion mutations in the other helicase domains, and a deletion in the potential helix-turn-helix DNA-binding motif fail to complement the ERCC3 excision repair defect of rodent group 3 mutants, which implies that the helicase domains as well as the potential DNA-binding motif are required for the repair function of ERCC3. Analysis of carboxy-terminal deletions suggests that the carboxy-terminal exon may comprise a distinct determinant for the DNA repair function. In addition, we show that a functional epitope-tagged version of ERCC3 accumulates in the nucleus. Deletion of the putative nuclear location signal impairs neither the nuclear location nor the repair function, indicating that other sequences may (also) be involved in translocation of ERCC3 to the nucleus.
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PMID:Mutational analysis of ERCC3, which is involved in DNA repair and transcription initiation: identification of domains essential for the DNA repair function. 819 50

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.
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PMID:Multifunctional RNA polymerase II initiation factor delta from rat liver. Relationship between carboxyl-terminal domain kinase, ATPase, and DNA helicase activities. 839 38