Tertiary structure of tRNAPhe. A possible correlation between the structural functional unit of this tRNA and its exonic sequence.
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.
D001483:Base Sequence; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl; D013329:Structure-Activity Relationship; D015003:Yeasts / Q000032:analysis
D012346:RNA, Transfer, Amino Acyl