Lacey J C, Wickramasinghe N S, Cook G W
Department of Biochemistry, University of Alabama, Birminghanm 35294.
Orig Life Evol Biosph. 1992;22(5):243-75. doi: 10.1007/BF01810856.
This article is an update of our earlier review (Lacey and Mullins, 1983) in this journal on the origin of the genetic code and the process of protein synthesis. It is our intent to discuss only experimental evidence published since then although there is the necessity to mention the old enough to place the new in context. We do not include theoretical nor hypothetical treatments of the code or protein synthesis. Relevant data regarding the evolution of tRNAs and the recognition of tRNAs by aminoacyl-tRNA-synthetases are discussed. Our present belief is that the code arose based on a core of early assignments which were made on a physico-chemical and anticodonic basis and this was expanded with new assignments later. These late assignments do not necessarily show an amino acid-anticodon relatedness. In spite of the fact that most data suggest a code origin based on amino acid-anticodon relationships, some new data suggesting preferential binding of Arg to its codons are discussed. While information regarding coding is not increasing very rapidly, information regarding the basic chemistry of the process of protein synthesis has increased significantly, principally relating to aminoacylation of mono- and polyribonucleotides. Included in those studies are several which show stereoselective reactions of L-amino acids with nucleotides having D-sugars. Hydrophobic interactions definitely play a role in the preferences which have been observed.
本文是我们早期发表在本期刊上关于遗传密码起源和蛋白质合成过程综述(莱西和穆林斯,1983年)的更新。我们的目的是只讨论自那时以来发表的实验证据,尽管有必要提及那些年代久远的证据以便将新证据置于背景之中。我们不包括对密码或蛋白质合成的理论或假设性论述。讨论了有关tRNA进化以及氨酰-tRNA合成酶对tRNA识别的相关数据。我们目前的看法是,密码基于早期在物理化学和反密码子基础上做出的核心分配而产生,后来随着新的分配而扩展。这些后期分配不一定显示出氨基酸与反密码子的相关性。尽管大多数数据表明密码起源基于氨基酸与反密码子的关系,但也讨论了一些新数据,这些数据表明精氨酸与其密码子的优先结合。虽然关于编码的信息增长并不迅速,但关于蛋白质合成过程基础化学的信息有了显著增加,主要涉及单核苷酸和多核苷酸的氨酰化。这些研究包括几项显示L-氨基酸与具有D-糖的核苷酸发生立体选择性反应的研究。疏水相互作用肯定在已观察到的偏好中起作用。