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Isolation and characterization of cDNA encoding mouse RNA polymerase II subunit RPB14
Institution:1. Lithosphere Fluid Research Lab, Faculty of Science, ELTE Eötvös Loránd University, Pázmány P. stny. 1/C, Budapest H–1117, Hungary;2. Doctoral School of Environmental Sciences, Faculty of Science, ELTE Eötvös Loránd University, Pázmány P. stny. 1/C, Budapest H–1117, Hungary;3. O&GD Central Ltd., Lövőház u. 39, Budapest H–1024, Hungary;4. Department of Chemical and Environmental Process Engineering, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H–1111, Hungary;5. Sand Hill Petroleum B.V., Cantonlaan 4, Baarn 3742 CJ, Netherlands;6. Institute of Earth Physics and Space Science, Eötvös Loránd Research Network, Csatkai Endre u. 6-8, Sopron H–9400, Hungary;7. Supervisory Authority for Regulatory Affairs, Columbus u. 17-23, Budapest H–1145, Hungary;8. Centre of Environmental Sciences, Faculty of Science, ELTE Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest H–1117, Hungary;1. CIRI, Centre International de Recherche en Infectiologie, Team Autophagy Infection Immunity, Université de Lyon, Inserm U1111, Université Claude Bernard Lyon 1, CNRS, UMR5308, ENS de Lyon, F-69007, Lyon, France;2. Department of Pediatric Hepatology, Gastroenterology and Nutrition, Femme-Mère-Enfant Hospital, Hospices Civils de Lyon, Bron, France;3. Department of Gastroenterology, Lyon Sud Hospital, Hospices Civils de Lyon, Lyon, France;4. Equipe Labellisée par la Fondation pour la Recherche Médicale, FRM, France;1. University of Maribor, Faculty of Civil Engineering, Transportation Engineering and Architecture, Smetanova 17, Maribor 2000, Slovenia;2. Institute of Mathematics, Physics and Mechanics, Jadranska 19, Ljubljana 1000, Slovenia;3. University of Maribor, Faculty of Energy Technology, Hočevarjev trg 1, Krško 8270, Slovenia;4. CAMTP-Center for Applied Mathematics and Theoretical Physics, University of Maribor, Krekova 2, Maribor SI-2000, Slovenia;5. Instituto de Ciências Matemáticas e de Computação, Universidade de São Paulo, Avenida Trabalhador São-carlense, 400-13566-590, São Carlos, Brazil;6. University of Maribor, Faculty of Natural Science and Mathematics, Koroška 160, Maribor 2000, Slovenia
Abstract:By means of the yeast two-hybrid system using the 40-kDa subunit of mouse RNA polymerase I, mRPA40, as the bait, we isolated a mouse cDNA which encoded a protein with significant homology in amino acid sequence to the 12.5-kDa subunit of Saccharomyces cerevisiae RNA polymerase II, B12.5 (RPB11). Specific antibody raised against the recombinant protein that was derived from the cDNA reacted with a 14-kDa polypeptide in highly purified mammalian RNA polymerase II and did not react with any subunit of RNA polymerase I or III. Moreover, the antibody co-immunoprecipitated the largest subunit of mouse RNA polymerase II. These results provide biochemical evidence that the cDNA isolated, named mRPB14, encodes a specific subunit of RNA polymerase II, and indicate that the subunit organization of the enzyme is conserved between yeast and mouse. A possible role of the α-motif Dequard-Chablat, M., Riva, M., Carles, C. and Sentenac, A., J. Biol. Chem. 266 (1991) 15300–15307] in the protein-protein interaction between mRPA40 and mRPB14 is also discussed.
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