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Aminoacyl-tRNA synthetase families and their significance to the origin of the genetic code (1978)

Wetzel, Ronald

Springer

Origins of life and evolution of the biospheres 9 (1978), S. 39-50

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ISSN: 1573-0875

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Geosciences

Notes: Abstract A correlation of various aspects of the protein structures and substrate and mechanistic specificities of the aminoacyl-tRNA synthetases has led to the identification of at least one family of enzymes probably derived from a common ancestral synthetase. While strong correlations exist only in one part of the array of 64 codons comprising the Genetic Code, this itself may be interpreted as a meaningful pattern, most consistent with a development of the present code from earlier codes containing fewer amino acids and fewer available codons. Specifically, strong correlations in the enzymes whose cognate tRNAs respond to codons containing a central pyrimidine, including the enzyme family of Ile-, Phe-, Val-, Met-, and Leu-tRNA synthetases, suggests that these enzymes evolved last, and that, therefore, an earlier version of the Genetic Code was comprised solely of codons containing a central purine. It is suggested that further study of the historical interrelationships of these enzymes could lead to a fairly detailed picture of how the Genetic Code developed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00929712

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Identification and nucleotide sequence of the sup8-e UGA-suppressor leucine tRNA from Schizosaccharomyces pombe (1979)

Wetzel, Ronald ; Kohli, Jürg ; Altruda, Fiorella ; [et al.]

Springer

Molecular genetics and genomics 172 (1979), S. 221-228

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ISSN: 1617-4623

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Using the translation of rabbit globin mRNA in wheat germ extracts as an assay for ochre and opal suppression, a UGA suppressor tRNA from Schizosaccharomyces pombe strain sup8-e was purified by column chromatography and two-dimensional gel electrophoresis. The purified tRNA can be aminoacylated with leucine by a crude aminoacyl-tRNA synthetase preparation from a wild type S. pombe strain, and has high activity in the suppressor assay. By a combination of post-labeling fingerprinting and rapid gel sequencing methods the nucleotide sequence of this suppressor tRNA was determined to be: pG-C-G-G-C-U-A-U-G-C-C-ac4C-G-A-G-D-G-D-G-D-A-A-G-G-G-m 2 2 G-G-C-A-G-A-Ψ-U-U*-C-A-m1G-C-C-C-U-G-C-U-G-U-U-G-U-A-A-A-A-C-G-m5C-G-A-G-A-G-T-Ψ-C-G-m1A-A-C-C-U-C-U-C-U-G-G-C-C-G-C-A-C-C-AOH. The anticodon sequence U*CA is complementary to the UGA codon. An interesting feature of the suppressor tRNA is an expanded anticodon loop of nine nucleotides owing to an A-C nonpair at the first anticodon stem position.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00268286

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