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Effect of Nascent Peptide Steric Bulk on Elongation Kinetics in the Ribosome Exit Tunnel

机译:新生肽式块体对核糖肿瘤隧道伸长动力学的影响

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Abstract All proteins are synthesized by the ribosome, a macromolecular complex that accomplishes the life-sustaining tasks of faithfully decoding mRNA and catalyzing peptide bond formation at the peptidyl transferase center (PTC). The ribosome has evolved an exit tunnel to host the elongating new peptide, protect it from proteolytic digestion, and guide its emergence. It is here that the nascent chain begins to fold. This folding process depends on the rate of translation at the PTC. We report here that besides PTC events, translation kinetics depend on steric constraints on nascent peptide side chains and that confined movements of cramped side chains within and through the tunnel fine-tune elongation rates. Graphical Abstract Display Omitted Highlights ? A systematic increase of side-chain size induces rank-order slowing of elongation rate in upper, but not lower, tunnel regions. ? Increased side-chain volume leads to increased van der Waals interactions between nascent peptide and ribosome tunnel. ? A two-step translation strategy was developed to evaluate the effects of bulky side chains on elongation kinetics.
机译:摘要所有蛋白质由核糖体合成,核糖体合成,该蛋白质复合体,其达到富肽解码mRNA和催化肽转移酶中心(PTC)催化肽键形成的寿命维持任务。核糖体已经进化出一个出口隧道以托管伸长的新肽,保护其免受蛋白水解消化,并引导其出现。这是新生链开始折叠。这种折叠过程取决于PTC的翻译速率。我们在此报告,除了PTC事件,翻译动力学依赖于新生肽侧链上的空间约束,并且在隧道微调伸长率内部和通过隧道狭窄侧链的狭窄运动。图形抽象显示省略了亮点?侧链尺寸的系统增加诱导上部,但不低,隧道区域的伸长率的秩序速度。还是增加的侧链体积导致泛染肽和核糖体隧道之间的范德华相互作用增加。还是开发了一种两步翻译策略,以评估庞大的侧链对伸长动力学的影响。

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