Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0694563 (eds)
 1,062 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A 569-base pair fragment encompassing the upstream regulatory region, the RNA initiation sites, and the initial part of the coding region of the Saccharomyces cerevisiae alcohol dehydrogenase II gene has been analyzed for the presence of sites which undergo conformational modification under torsional stress. Fine mapping of P1 and S1 endonuclease-sensitive sites was obtained on single topoisomers produced by in vitro ligation. It was shown that the upstream activator sequence, the TATA sequence, a region directly upstream to the RNA initiation sites, and several positions in the first segment of the transcribed region change conformation as a function of the applied torsional stress in a precisely coordinate fashion. The superhelical density optima for this coordinate modifications have been determined. Analysis of the conformational changes of the promoter sequence in several naturally occurring (Young, E. T., Williamson, V. M., Taguchi, A., Smith, M., Sledziewski, L., Russel, D., Osterman, J., Denis, C., Cox, D., and Beier, D., (1982) in Genetic Engineering of Microorganisms for Chemicals (Hollander, A., De Moss, R. D., Kaplan, S., Konisky, J., Savage, D., and Wolle, R. S., eds) pp. 335-361, Plenum Publishing Corp., New York) up-promoter constitutive mutants was performed. This analysis has shown that the conformation of functionally relevant sites changes as a function of sequence mutations that have taken place elsewhere; this shows that the conformational behavior of the whole promoter region is linked and suggests transmission in cis of topological effects in RNA polymerase II promoters.
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PMID:The intrinsic topological information of the wild-type and of up-promoter mutations of the Saccharomyces cerevisiae alcohol dehydrogenase II regulatory region. 305 83

Transcription from class II promoters requires five general factors, IIA, IIB, IID, IIE, and IIF, in addition to RNA polymerase II for basal levels of transcription (Reinberg, D., Flores, O., and Buckbinder, L. (1987) in Molecular Biology of RNA: New Perspectives (Inouye, M., and Dudock, B., eds) pp. 423-439, Academic Press, Orlando, FL). A protein fraction containing transcription factors (TF) IIE and IIF was able to reconstitute transcription from the adenovirus major late promoter when added to extracts depleted of the RNA polymerase II-associating proteins RAP 30 and RAP 74 (Sopta, M., Carthew, R.W., and Greenblatt, J. (1985) J. Biol. Chem. 260, 10353-10360). Studies with monoaffinity-purified antibodies directed against RAP 30 demonstrated, by Western blot analysis, that RAP 30 copurifies on five columns with transcription factor IIF. That RAP 30 is a functional component of TFIIF was also demonstrated; preincubation of anti-RAP 30 antibodies with purified TFIIF inhibited transcription. Inhibition of transcription was overcome by the addition of purified TFIIF. RAP 30 is an integral part of a preinitiation complex; the incubation of all the general transcription factors with a promoter-containing DNA, prior to the addition of the anti-RAP 30 antibodies, resulted in the formation of a DNA-protein complex that was not inhibited by the antibodies. Incubation of the transcription factors in the absence of a promoter-containing DNA resulted in a complex that was partially resistant to the antibodies.
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PMID:Factors involved in specific transcription by mammalian RNA polymerase II. RNA polymerase II-associating protein 30 is an essential component of transcription factor IIF. 339 44

Polyclonal antibodies to calf thymus RNA polymerase II were raised in laying hens. Up to 75 mg of immunoglobulin/egg yolk were extracted by the polyethylene glycol procedure of Roeder (Roeder, R.G. (1976) in RNA Polymerase (Losick, R., and Chamberlin, M., eds) pp. 285-330, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY). The concentration of specific antibody in egg yolks (IgY) was comparable to that of serum as measured by enzyme-linked immunoassay. Purified antibody was shown to be directed against enzyme by removal of enzyme activity in immune complexes precipitated by rabbit anti-chicken IgY. The antibodies recognized several of the subunits of the enzyme as determined by their reactivity with polypeptides transferred to nitrocellulose paper after gradient sodium dodecyl sulfate-gel electrophoresis. Production of antibodies in laying hens may facilitate the study of other highly conserved antigens that are poorly immunogenic in mammalian hosts.
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PMID:Antibodies to calf thymus RNA polymerase II from egg yolks of immunized hens. 633 47