Dea P, Alta M, Patt S, Schweizer M P
Nucleic Acids Res. 1978 Feb;5(2):307-15. doi: 10.1093/nar/5.2.307.
360 MHz measurements of chemical shifts, 3J1'-2', and T1 as a function of temperature for various protons of the hexanucleotide 2'-OMeGpApApYpAppsi from torula yeast tRNAphe have revealed a unique involvement of the Yt base in the structure and conformation of this oligonucleotide. Whereas the adenosine residues in the anticodon triplet are relatively stable to temperature increase, the Yt readily undergoes destacking and a change in ribose conformation. The destacking most likely involves a torsional displacement of the Yt base occasioned by a rotation of the phosphate-ribose backbone. The possible relevance of this unusual behavior to the influence of the Yt residue in tRNA function in protein biosynthesis is discussed.
对来自啤酒酵母苯丙氨酸tRNA的六核苷酸2'-OMeGpApApYpAppsi的各种质子进行了360兆赫的化学位移、3J1'-2'以及作为温度函数的T1测量,结果揭示了Yt碱基在该寡核苷酸结构和构象中独特的作用。虽然反密码子三联体中的腺苷残基对温度升高相对稳定,但Yt很容易发生解堆积以及核糖构象的改变。这种解堆积很可能涉及由磷酸核糖主链旋转引起的Yt碱基的扭转位移。本文讨论了这种异常行为与Yt残基对蛋白质生物合成中tRNA功能影响的可能相关性。