Malathi R, Yathindra N
Biochem J. 1984 Apr 1;219(1):341-4. doi: 10.1042/bj2190341.
It has been shown recently [Go (1981) Nature (London) 291, 90-92; Blake (1983) Trends Biochem Sci. 8, 11-13] that the exonic regions of the genes of proteins haemoglobin, lysozyme and immunoglobin correspond closely to the compactly folded structural units. Despite the absence of classical domain structures in tRNA compared with those found in several proteins, close inspection of certain features in the distance maps obtained for yeast tRNAPhe using the conformationally equivalent heminucleotide scheme reveals that a similar situation might also be present in ribonucleic acids such as tRNA species and the exonic sequences of their genes. Also it seems possible that certain segments of yeast tRNAPhe may be characterized as possessing a domain-like character, and this seems to provide stereochemical support for possible conservation of L-shape structure for tRNA species lacking the entire dihydrouridine arm such as those found in mitochondria.
最近的研究表明[戈（1981年），《自然》（伦敦）291卷，90 - 92页；布莱克（1983年），《生物化学趋势》8卷，11 - 13页]，血红蛋白、溶菌酶和免疫球蛋白等蛋白质基因的外显子区域与紧密折叠的结构单元密切对应。尽管与几种蛋白质中的经典结构域结构相比，tRNA中不存在这种结构，但使用构象等效的半核苷酸方案对酵母苯丙氨酸tRNA获得的距离图中的某些特征进行仔细检查后发现，在诸如tRNA种类及其基因的外显子序列等核糖核酸中可能也存在类似情况。此外，酵母苯丙氨酸tRNA的某些片段似乎可能具有类似结构域的特征，这似乎为缺乏完整二氢尿嘧啶臂的tRNA种类（如线粒体中发现的那些）可能保留L形结构提供了立体化学支持。
