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蛋白质生物合成的第四步:翻译终止后复合物的解体 被引量:1

The Fourth Step of Protein Synthesis: Disassembly of The Posttermination Complex
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摘要 蛋白质合成过程一般被归纳为由合成的起始、肽链的延伸和合成的终止组成的三步曲.然而,随着对核糖体再循环因子(ribosomerecyclingfactor,RRF)在蛋白质合成过程中作用的深入研究,人们提出了蛋白质生物合成应是四步曲,这第四步就是翻译终止后核糖体复合物的解体,也就是通常说的核糖体循环再利用.简要地介绍了翻译终止后复合物解体的可能机制:核糖体再循环因子和蛋白质合成延伸因子G在核糖体上协同作用催化这一过程的完成. Protein synthesis is generally known as consisting of three steps: initiation, elongation, and termination. Much less known is the fourth step: disassembly of the posttermination ribosomal complex and recycling of the machinery necessary for the next round of translation. In bacteria, after reaching the end of a protein-coding sequence, the ribosome binds release factor RF-1 or RF-2 in response to stop codon in the ribosomal A site, activating hydrolysis of the polypeptide chain from peptidyl-tRNA. Release factor RF-3 then catalyzes dissociation of RF-1 or RF-2, leaving a posttermination complex consisting of the 70S ribosome, mRNA, and deacylated tRNA in the P site. How the posttermination complex is disassembled for next round of protein synthesis is a very basic process. The possible mechanisms of posttermination complex disassembly during protein synthesis was summarized: the forth step of protein synthesis is catalyzed by the concerted action of ribosome recycling factor (RRF) and elongation factor G (EF-G).
出处 《生物化学与生物物理进展》 SCIE CAS CSCD 北大核心 2005年第6期483-489,共7页 Progress In Biochemistry and Biophysics
关键词 翻译终止后核糖体复合物的解体 核糖体再循环因子 延伸因子G posttermination ribosomal complex disassembly ribosome recycling factor elongation factor G
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  • 1Selmer M, Al-Karadaghi S, Hirokawa G, et al. Crystal structure of Thermotoga maritima ribosome recycling factor:,a tRNA mimic.Science, 1999, 286(5448): 2349-2352.
  • 2Kim K K, Min K, Sub S W. Crystal structure of the ribosome recycling factor from Escherichia coll. EMBO J, 2000,19(10):2362-2370.
  • 3Toyoda T, Tin O F, Ito K, et al. Crystal structure combined with genetic analysis of the Thermm thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch.RNA, 2000, 6(10):1432-1444.
  • 4Nakano H, Yoshida T, Uchiyama S, et al. Structure and binding mode of a ribosome recycling factor CRRF) from mesophilic bacterium. J Biol Chem, 2003, 278(5):3427-3436.
  • 5Saikrishnan K, Kalapala S K, Varshney U, et al. X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications. J Mol Biol, 2005, 345(1):29-38.
  • 6Yoshida T, Uchiyama S, Nakano H, et al. Solution structure of the ribosome recycling factor from Aquifex aeolicus. Biochemistry,2001, 40(8):2387-2396.
  • 7Nakamura Y, Ito IC Making sense of mimic in translation termination. Trends Biochem Sci, 2003, 28(2):99-105.
  • 8Kaji A, Kiel M C, Hirokawa G, et al. The fourth step of protein synthesis: disassembly of the posttermination complex is catalyzed by elongation factor G and ribosome recycling factor, a near-perfect mimic of tRNA. Cold Spring Harb Symp Quant Biol, 2001, 66:515-529.
  • 9Lancaster L, Kiel M C, Kaji A, et al. Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell, 2002, 111(1):129-140.
  • 10Agrawal R K, Sharma M R, Kiel M C, et al. Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome:functional implications. Proc Natl Acad Sci USA,2004,101(24):8900-8905.

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