Single-molecule investigation of the T4 bacteriophage DNA polymerase holoenzyme: multiple pathways of holoenzyme formation.
作者： R. Derike Smiley , Zhihao Zhuang , Stephen J. Benkovic , Gordon G. Hammes
DOI: 10.1021/BI0603322
关键词: Polymerase 、 DNA replication 、 DNA clamp 、 Processivity 、 DNA polymerase delta 、 DNA polymerase 、 DNA polymerase II 、 Replisome 、 Biology 、 Biophysics 、 Biochemistry
摘要: In T4 bacteriophage, the DNA polymerase holoenzyme is responsible for accurate and processive synthesis. The consists of gp43 clamp protein gp45. To form a productive complex, loader gp44/62 required loading gp45, along with MgATP, also subsequent binding to loaded clamp. Recently published evidence suggests that assembly in replisome may take place via more than one pathway [Zhuang, Z., Berdis, A. J., Benkovic, S. J. (2006) Biochemistry 45, 7976-7989]. demonstrate unequivocally whether there are multiple pathways leading formation holoenzyme, single-molecule fluorescence microscopy has been used study potential on substrate. results obtained reveal four foster functional DNA: (1) loader-clamp complex followed by polymerase, (2) then (3) (4) complex. all cases, MgATP required. possible physiological significance various discussed context replication initiation lagging strand synthesis during stages phage replication.
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sci-hub.se 参考文章(23)
P. T. R. Rajagopalan, Z. Zhang, L. McCourt, M. Dwyer, S. J. Benkovic, G. G. Hammes, Interaction of dihydrofolate reductase with methotrexate: Ensemble and single-molecule kinetics Proceedings of the National Academy of Sciences of the United States of America. ,vol. 99, pp. 13481- 13486 ,(2002) , 10.1073/PNAS.172501499
Michael A. Trakselis, Anthony J. Berdis, Stephen J. Benkovic, Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme Journal of Molecular Biology. ,vol. 326, pp. 435- 451 ,(2003) , 10.1016/S0022-2836(02)01330-X
Gisela Mosig, Nancy Colowick, Michael E. Gruidl, Ardith Chang, Alex J. Harvey, Multiple initiation mechanisms adapt phage T4 DNA replication to physiological changes during T4's development Fems Microbiology Reviews. ,vol. 17, pp. 83- 98 ,(1995) , 10.1111/J.1574-6976.1995.TB00190.X
Barbara Fenn Kaboord, Stephen J. Benkovic, Accessory proteins function as matchmakers in the assembly of the T4 DNA polymerase holoenzyme Current Biology. ,vol. 5, pp. 149- 157 ,(1995) , 10.1016/S0960-9822(95)00036-4
B M Alberts, J R Piperno, An ATP stimulation of T4 DNA polymerase mediated via T4 gene 44/62 and 45 proteins. The requirement for ATP hydrolysis. Journal of Biological Chemistry. ,vol. 253, pp. 5174- 5179 ,(1978) , 10.1016/S0021-9258(17)34673-2
T C Jarvis, J W Newport, P H von Hippel, Stimulation of the processivity of the DNA polymerase of bacteriophage T4 by the polymerase accessory proteins. The role of ATP hydrolysis. Journal of Biological Chemistry. ,vol. 266, pp. 1830- 1840 ,(1991) , 10.1016/S0021-9258(18)52369-3
N G Nossal, DNA replication with bacteriophage T4 proteins. Purification of the proteins encoded by T4 genes 41, 45, 44, and 62 using a complementation assay. Journal of Biological Chemistry. ,vol. 254, pp. 6026- 6031 ,(1979) , 10.1016/S0021-9258(18)50514-7
T Tsurimoto, B Stillman, Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis Journal of Biological Chemistry. ,vol. 266, pp. 1961- 1968 ,(1991) , 10.1016/S0021-9258(18)52386-3
Stephen C. Alley, Vincent K. Shier, Ernesto Abel-Santos, Daniel J. Sexton, Patrice Soumillion, Stephen J. Benkovic, Sliding Clamp of the Bacteriophage T4 Polymerase Has Open and Closed Subunit Interfaces in Solution Biochemistry. ,vol. 38, pp. 7696- 7709 ,(1999) , 10.1021/BI9827971
Jun Xi, Zhihao Zhuang, Zhiquan Zhang, Tzvia Selzer, Michelle M. Spiering, Gordon G. Hammes, Stephen J. Benkovic, Interaction between the T4 helicase-loading protein (gp59) and the DNA polymerase (gp43): a locking mechanism to delay replication during replisome assembly. Biochemistry. ,vol. 44, pp. 2305- 2318 ,(2005) , 10.1021/BI0479508