STRUCTURAL DOMAINS OF TRANSFER-RNA MOLECULES
STRUCTURAL DOMAINS OF TRANSFER-RNA MOLECULES
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DOI:
10.1126/science.790568
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发表时间:
1976-01-01
期刊:
影响因子:
56.9
通讯作者:
RICH, A
中科院分区:
文献类型:
--
作者:
QUIGLEY, GJ;RICH, A
Various detailed features of the conformation of yeast tRNAPhe revealed by recent refinement analysis of X-ray diffraction data at 2.5 .ANG. resolution were described. The gross features of the molecule observed in the unrefined version were largely confirmed and a number of new features found. The unique role of the ribose 2'' hydroxyl groups in maintaining a series of nonhelical conformations in this RNA molecule has become apparent. Many of these features are a direct consequence of the geometry of the ribose phosphate backbone of RNA molecules, and these may also be found in structural regions of other RNA species as well. Special attention was directed toward 2 conformational motifs revealed by this analysis. These include the striking similarity between the T.psi.C and anticodon hairpin turns in the polynucleotide chain, which are stabilized by the participation of uridine in the U turn. In addition, there is frequent occurrence of an arch conformation in the polynucleotide chain which is stabilized by hydrogen bonds from 2'' hydroxyl residues to phosphate groups across the base of the arch. The importance of the 2'' hydroxyl interactions in defining tertiary structure is illustrated by the fact that, in the nonhelical regions, almost half of the ribose residues are involved in O2'' hydrogen-bonding interactions which stabilize the conformation of the molecule. Two regions which may have considerable functional significance during protein synthesis are described in detail. One involves the joining of the T.psi.C and D loops, which may undergo conformational change in the ribosome during protein synthesis. The other region is the anticodon, which seems conformationally poised, ready to interact with a single-stranded polynucleotide mRNA. Analysis of this end of the molecule suggests ways in which the anticodon may interact with the message, although as yet not enough is known to understand how 2 tRNA molecules interact with adjoining codons on the message.