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The effect of aging on cell-free protein synthesis in the free-living nematode Turbatrix aceti.

作者信息

Egilmez N K, Rothstein M

出版信息

Biochim Biophys Acta. 1985 Jul 5;840(3):355-63. doi: 10.1016/0304-4165(85)90215-6.

DOI:10.1016/0304-4165(85)90215-6
PMID:3847281
Abstract

The age-related reduction in cell-free protein synthesis in the free-living nematode Turbatrix aceti is due to a defect in the ribosomes. Addition of young ribosomal wash or use of young medium does not improve the activity of old, run-off ribosomes in the presence of phenylalanine and poly(U). It appears that some of the old ribosomes are incapable of binding the EF-1-GTP-aminoacyl-tRNA complex. These ineffective ribosomes are present in the 80 S (monosomal) fraction. Old ribosomes obtained from polysomes appear to bind normally.

摘要

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The effect of aging on cell-free protein synthesis in the free-living nematode Turbatrix aceti.
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2
[Stoichiometry of GTP hydrolysis during peptide synthesis on the ribosome. GTP hydrolysis uncoupled with ribosomal peptide synthesis and dependent on preparation of elongation factor T].[核糖体上肽合成过程中GTP水解的化学计量学。GTP水解与核糖体肽合成解偶联且依赖于延伸因子T的制备]
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Hydrolysis of GTP on elongation factor Tu.ribosome complexes promoted by 2'(3')-O-L-phenylalanyladenosine.2'（3'）-O-L-苯丙氨酰腺苷促进延伸因子Tu-核糖体复合物上GTP的水解。
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The accuracy of protein biosynthesis is limited by its speed: high fidelity selection by ribosomes of aminoacyl-tRNA ternary complexes containing GTP[gamma S].蛋白质生物合成的准确性受其速度限制：核糖体对含有鸟苷三磷酸γ-硫代物（GTP[γS]）的氨酰-tRNA三元复合物进行高保真选择。
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Binding of aminoacyl-tRNA to ribosomes promoted by elongation factor Tu. Studies on the role of GTP hydrolysis.延伸因子Tu促进氨酰tRNA与核糖体的结合。关于GTP水解作用的研究。
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