Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer
Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer
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DOI：
10.1093/emboj/19.19.5241
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发表时间：
2000-10-02
期刊：
影响因子：
11.4
通讯作者：
Nierhaus, KH
中科院分区：
文献类型：
--
作者：
Diedrich, G;Spahn, CMT;Nierhaus, KH
核糖体蛋白L2、L3和L4与23S RNA一起是催化50S亚基上的肽键形成的主要候选者。L2在进化上高度保守，这使得我们对缺乏L2或携带突变的L2的重构50S颗粒进行了彻底的功能分析。L2在50S亚基的组装或在肽基转移酶中心的tRNA的3 '末端的固定中不起主导作用。然而，它是30S和50S亚基结合所必需的，并且强烈参与tRNA与A和P位点的结合，可能在tRNA手肘区域。此外，虽然保守的组氨酰残基229对肽基转移酶活性极其重要，但它显然不参与其他测量功能。其他诱变氨基酸（H14、D83、S177、D228、H231）均未表现出这种强烈且排他性的参与肽键形成。这些结果被用来严格审查建议的直接参与His229在催化肽合成。
Ribosomal proteins L2, L3 and L4, together with the 23S RNA, are the main candidates for catalyzing peptide bond formation on the 50S subunit, That L2 is evolutionarily highly conserved led us to perform a thorough functional analysis with reconstituted 50S particles either lacking L2 or harboring a mutated L2. L2 does not play a dominant role in the assembly of the 50S subunit or in the fixation of the 3'-ends of the tRNAs at the peptidyl-transferase center. However, it is absolutely required for the association of 30S and 50S subunits and is strongly involved in tRNA binding to both A and P sites, possibly at the elbow region of the tRNAs, Furthermore, while the conserved histidyl residue 229 is extremely important for peptidyl-transferase activity, it is apparently not involved in other measured functions. None of the other mutagenized amino acids (H14, D83, S177, D228, H231) showed this strong and exclusive participation in peptide bond formation. These results are used to examine critically the proposed direct involvement of His229 in catalysis of peptide synthesis.