Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Steady state kinetic analysis of ATP hydrolysis.
作者： G.M. Weinstock , K. McEntee , I.R. Lehman
DOI: 10.1016/S0021-9258(19)68922-2
关键词:
摘要: The DNA-dependent ATPase activity of the recA protein Escherichia coli shows a complex dependence on ATP concentration. With single-stranded (SS) DNA cofactor, Hill coefficient for is 3.3 at pH 8.1 and 1.4 6.2. double-stranded (DS) 6.2 (no reaction detectable 8.1). In presence SS DNA, Km 20 microM, independent pH, while with DS 6.2, KmATP 100 microM. These other observations indicate that interaction influenced by both cofactor. ADP, UTP, dTTP, GTP are competitive inhibitors protein, indicating there single binding site nucleoside triphosphates. Nucleoside triphosphates, but not reduce hydrolysis thus can contribute to cooperative effect ATP.
sci-hub.st 参考文章(10)
G.M. Weinstock, K. McEntee, I.R. Lehman, Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis. Journal of Biological Chemistry. ,vol. 256, pp. 8829- 8834 ,(1981) , 10.1016/S0021-9258(19)68920-9
K. McEntee, G.M. Weinstock, I.R. Lehman, DNA and nucleoside triphosphate binding properties of recA protein from Escherichia coli. Progress in Nucleic Acid Research and Molecular Biology. ,vol. 26, pp. 265- 279 ,(1981) , 10.1016/S0079-6603(08)60411-0
G.M. Weinstock, K. McEntee, I.R. Lehman, Interaction of the recA protein of Escherichia coli with adenosine 5'-O-(3-thiotriphosphate). Journal of Biological Chemistry. ,vol. 256, pp. 8850- 8855 ,(1981) , 10.1016/S0021-9258(19)68923-4
K. McEntee, G.M. Weinstock, I.R. Lehman, Binding of the recA protein of Escherichia coli to single- and double-stranded DNA Journal of Biological Chemistry. ,vol. 256, pp. 8835- 8844 ,(1981) , 10.1016/S0021-9258(19)68921-0
K. McEntee, G. M. Weinstock, I. R. Lehman, Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 76, pp. 2615- 2619 ,(1979) , 10.1073/PNAS.76.6.2615
T. Shibata, C. DasGupta, R. P. Cunningham, C. M. Radding, Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 76, pp. 1638- 1642 ,(1979) , 10.1073/PNAS.76.4.1638
C. M. Radding, T. Shibata, R. P. Cunningham, C. DasGupta, Homologous pairing in genetic recombination: complexes of recA protein and DNA. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 76, pp. 5100- 5104 ,(1979) , 10.1073/PNAS.76.10.5100
Richard P. Cunningham, Takehiko Shibata, Chanchal DasGupta, Charles M. Radding, Single strands induce recA protein to unwind duplex DNA for homologous pairing Nature. ,vol. 281, pp. 191- 195 ,(1979) , 10.1038/281191A0
G. M. Weinstock, K. McEntee, I. R. Lehman, ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. ,vol. 76, pp. 126- 130 ,(1979) , 10.1073/PNAS.76.1.126
T. Ogawa, H. Wabiko, T. Tsurimoto, T. Horii, H. Masukata, H. Ogawa, Characteristics of purified recA protein and the regulation of its synthesis in vivo. Cold Spring Harbor Symposia on Quantitative Biology. ,vol. 43, pp. 909- 915 ,(1979) , 10.1101/SQB.1979.043.01.099