Nucleotide Sequence of
            <i>Escherichia coli</i>
            Tyrosine Transfer Ribonucleic Acid

Doctor, Bhupendra P.; Loebel, J. E.; Sodd, Mary Ann; Winter, David B.

doi:10.1126/science.163.3868.693

Cited by 53 publications

(14 citation statements)

References 13 publications

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“…coli tyrosine tRNA sequences, Doctor et al [22] have proposed a sequence for E . coli B t R N A p which, although very similar to our tRNA I1 sequence, differs from the latter a t 7 nucleotide positions.…”

Section: Discussionmentioning

confidence: 99%

“…coli tyrosine tRNA could be separated into two species [ 11,201 suggested that two tyrosine tRNA species were present and that they differed in sequence by two nucleotides so that on T, ribonuclease digestion one gave UCAUCG and the other UCACAG. I n fact, Doctor and Nishimura have independently identified UCACAG from E. coli B tyrosine tRNA I1 [22,24].…”

Section: Total Tyrosine Trnas From E Colimentioning

confidence: 99%

See 1 more Smart Citation

The Nucleotide Sequences of Tyrosine Transfer RNAs of Escherichia coli

Goodman

Abelson

Landy

et al. 1970

European Journal of Biochemistry

133

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The tyrosine tRNAs specified by the E . coli amber suppressor gene su: , , and the wild type non-suppressing allele su,, were selectively labelled with 3 2 P in E . coli infected with transducing phage p80 carrying either of these genes. The determination of the nucleotide sequence of the S U :, , tyrosine tRNA is described. This tRNA has the anticodon CUA. The s u~, tRNA differs from su: , , tRNA by a single nucleotide and has the anticodon GUA where G is a modified guanylic acid residue. E . coli su-cells contain two tyrosine tRNAs (I and 11). The determination of the nucleotide sequence of these is described. Species I is identical to su,, tRNA while species I1 differs by two nucleotides in the variable loop region.

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Section: Discussionmentioning

confidence: 99%

Section: Total Tyrosine Trnas From E Colimentioning

confidence: 99%

The Nucleotide Sequences of Tyrosine Transfer RNAs of Escherichia coli

Goodman

Abelson

Landy

et al. 1970

European Journal of Biochemistry

133

View full text Add to dashboard Cite

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“…Furthermore, in those cases where the primary structure is known, the cytokinin is found immediately adjacent to the presumed anticodon (1,5,17). The continuing debate as to whether or not the physiological activity of exogenously supplied cytokinins is mediated by their presence in tRNA seems to have been recently resolved by the work of Chen and Hall (4).…”

Section: Introductionmentioning

confidence: 99%

The Metabolism and Biological Activity of a 9-Substituted Cytokinin

et al. 1971

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In order to test the metabolic stability of 9-substituted cytokinins, 6-benzylamino-9-methyl purine has been synthesized and labeled with 14C in the 9-methyl carbon or doubly labeled with 14C in the 9-methyl carbon and 3H in the methylene moiety of the side chain. Although the 6-benzylamino-9-methylpurine is chemically stable, cytokinin-requiring tissues begin removing the 9-substituent in as little as 10 minutes. Among the various metabolic products is free benzylaminopurine. Thus, the biological activity of 9-substituted cytokinins could be accounted for by their conversion to the free base.The widespread presence of cytokinins in the transfer RNA of animals, plants, and microorganisms is well established (see review by Key [14]). Furthermore, in those cases where the primary structure is known, the cytokinin is found immediately adjacent to the presumed anticodon (1,5,17). The continuing debate as to whether or not the physiological activity of exogenously supplied cytokinins is mediated by their presence in tRNA seems to have been recently resolved by the work of Chen and Hall (4). Here it was shown that the potent cytokinin N6-(A2-isopentenyl) adenosine occurs in the tRNA of cultivated tobacco tissue even though the tissue requires an exogenous cytokinin in order to grow. The fact that the cytokinin supplied in the medium is not the metabolic precursor of the cytokinin in the tRNA argues that the role of the former is distinct in at least some important way from that of the latter.This work, however, cannot be used as evidence against the notion that exogenous cytokinins act through their observed incorporation into polynucleotides (7, 9, 10). One would need to demonstrate that cytokinins which are prevented from entering into nucleotide formation nevertheless retain all of their biological activity. It occurred to us that the use of blocking agents at the 9 position of the purine moiety would result in compounds which might yield information concerning the relation between nucleotide formation and biological activity of the I

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“…It is not clear whether the occurrence of dihydrouridine in tRNA's is a result of the hydrogenation of uridine or of cytidine with subsequent deamination (Zachau, 1970). In the cloverleaf model which was proposed by Holley, Apgar, Everett, Madison, Marquisee, Merrill, Penswick & Zamir (1965) for the secondary structure of tRNA's, dihydrouridine is a regular constituent of the 'dihydrouridine loop' (for an exception see Doctor, Loebel, Sodd & Winter, 1969) but it also occurs in other non-helical, non-base-paired regions (Zachau, 1965). Since the role of the modified nucleosides in tRNA's is still uncertain we undertook the X-ray analysis described below to contribute to an understanding of the structural features of dihydrouridine.…”

Section: Introductionmentioning

confidence: 99%