Identity elements of<i>Saccharomyces cerevisiae</i>tRNA<sup>His</sup>

Nameki, Nobukazu; Asahara, Haruichi; Shimizu, Mikio; Okada, Norihiro; Himeno, Hyouta

doi:10.1093/nar/23.3.389

Cited by 73 publications

(69 citation statements)

References 45 publications

(59 reference statements)

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“…By contrast, in eukaryotes, G Ϫ1 is added posttranscriptionally by tRNA His guanylyltransferase, which is encoded in yeast by the essential THG1 gene (7), and it catalyzes the addition of a guanine nucleotide to the 5Ј end of tRNA His across from residue A 73 of the tRNA, the nucleotide immediately preceding the CCA 3Ј end (7)(8)(9). G Ϫ1 addition activity is crucial for aminoacylation of tRNA His in vivo (10), consistent with the demonstration that G Ϫ1 is necessary and sufficient for histidyl-tRNA synthetase activity in vitro (11)(12)(13).…”

supporting

confidence: 56%

“…There is no naturally occurring mature ppp-tRNA that would be a substrate for Thg1, and activation by adenylylation occurs only with 75-mer p-tRNA His through Thg1 recognition of the anticodon (14), consistent with the crucial role of G Ϫ1 -containing tRNA His in charging tRNA His in vitro (11)(12)(13) and in vivo (10). Furthermore, tRNA His nucleotide addition is restricted to a single guanosine residue because Thg1 adds only the single required G Ϫ1 opposite the discriminator A 73 (Figs.…”

Section: Discussionmentioning

confidence: 89%

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tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition

Jackman

Phizicky

2006

Proc. Natl. Acad. Sci. U.S.A.

118

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Yeast tRNA His guanylyltransferase, Thg1, is an essential protein that adds a single guanine to the 5 end (G ؊1) of tRNA His . This G؊1 residue is required for aminoacylation of tRNA His by histidyl-tRNA synthetase, both in vitro and in vivo. The guanine nucleotide addition reaction catalyzed by Thg1 extends the polynucleotide chain in the reverse (3-5) direction of other known polymerases, albeit by one nucleotide. Here, we show that alteration of the 3 end of the Thg1 substrate tRNA His unleashes an unexpected reverse polymerase activity of wild-type Thg1, resulting in the 3-5 addition of multiple nucleotides to the tRNA, with efficiency comparable to the G ؊1 addition reaction. The addition of G؊1 forms a mismatched G⅐A base pair at the 5 end of tRNA His , and, with monophosphorylated tRNA substrates, it is absolutely specific for tRNA His . By contrast, reverse polymerization forms multiple G⅐C or C⅐G base pairs, and, with preactivated tRNA species, it can initiate at positions other than ؊1 and is not specific for tRNA His . Thus, wild-type Thg1 catalyzes a templated polymerization reaction acting in the reverse direction of that of canonical DNA and RNA polymerases. Surprisingly, Thg1 can also readily use dNTPs for nucleotide addition. These results suggest that 3-5 polymerization represents either an uncharacterized role for Thg1 in RNA or DNA repair or metabolism, or it may be a remnant of an earlier catalytic strategy used in nature.polymerase ͉ Saccharomyces cerevisiae ͉ THG1 ͉ tRNA modification A ll known polymerases catalyze the addition of nucleotides in the 5Ј-3Ј direction, including classical DNA and RNA polymerases, as well as telomerase, reverse transcriptase, and a number of template-independent RNA polymerases (1-3). These polymerases universally catalyze the same reaction, involving attack by the polynucleotide 3Ј-OH on the

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supporting

confidence: 56%

Section: Discussionmentioning

confidence: 89%

tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition

Jackman

Phizicky

2006

Proc. Natl. Acad. Sci. U.S.A.

118

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“…By the way, this behavior may indicate that the recognition by a eukaryotic HisRS of either the anticodon of tRNA His or the pseudo-anticodon of plant viral RNAs tolerates noncognate triplets. Indeed, upon substitution of the anticodon in the Saccharomyces cereVisiae system, the decreases in aminoacylation efficiency do not exceed 70-fold (36). In another study, the anticodon loop of yeast tRNA was transplanted inside yeast tRNA Asp (31).…”

Section: Discussionmentioning

confidence: 97%

Function of the Extra 5‘-Phosphate Carried by Histidine tRNA

2000

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Among elongator tRNAs, tRNA specific for histidine has the peculiarity to possess one extra nucleotide at position -1. This nucleotide is believed to be responsible for recognition by histidyl-tRNA synthetase. Here, we show that, in fact, it is the phosphate 5' to the extra nucleotide which mainly supports the efficiency of the tRNA aminoacylation reaction catalyzed by Escherichia coli histidyl-tRNA synthetase. In the case of the reaction of E. coli peptidyl-tRNA hydrolase, this atypical phosphate is dispensable. Instead, peptidyl-tRNA hydrolase recognizes the phosphate of the phosphodiester bond between residues -1 and +1 of tRNA(His). Recognition of the +1 phosphate of tRNA(His) by peptidyl-tRNA hydrolase resembles, therefore, that of the 5'-terminal phosphate of other elongator tRNAs.

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“…Recent studies have shown that identity elements of a tRNA often vary during evolution (9)(10)(11)(12)(13)(14)(15)(16), although some are maintained (17)(18)(19)(20). An artificial aminoacylation system comprised of a tRNA and an aminoacyl-tRNA synthetase from different sources often causes a unilateral aminoacylation specificity and sometimes causes a lack of amino acid specificity (21)(22)(23).…”

Section: Introductionmentioning

confidence: 99%

Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae

Soma

Himeno

1998

Nucleic Acids Research

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Prokaryotes have three amino acid-specific class II tRNAs that possess a characteristic long variable arm, tRNA Ser , tRNA Leu and tRNA Tyr , while eukaryotes have only two, tRNA Ser and tRNA Leu . Because of such a phylogenetic divergence in the composition of tRNA, the class II tRNA system is a good candidate for studying how the tRNA recognition manner has evolved in association with the evolution of tRNA. We report here a cross-species aminoacylation study of the class II tRNAs, showing the unilateral aminoacylation specificity between Escherichia coli and a yeast, Saccharomyces cerevisiae. Both SerRS and LeuRS from E.coli were unable to aminoacylate yeast class II tRNAs; in contrast, the yeast counterparts were able to aminoacylate E.coli class II tRNAs. Yeast seryl-tRNA synthetase was able to aminoacylate not only E.coli tRNA Ser but also tRNA Leu and tRNA Tyr , and yeast LeuRS was able to aminoacylate not only E.coli tRNA Leu but also tRNA Tyr . These results indicate that the recognition manner of class II tRNA, especially the discrimination strategy of each aminoacyl-tRNA synthetase against noncognate class II tRNAs, is significantly divergent between E.coli and yeast. This difference is thought to be due mainly to the different composition of class II tRNAs in E.coli and yeast.

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Identity elements ofSaccharomyces cerevisiaetRNA^His

Cited by 73 publications

References 45 publications

tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition

tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition

Function of the Extra 5‘-Phosphate Carried by Histidine tRNA

Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae

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Identity elements ofSaccharomyces cerevisiaetRNAHis

Cited by 73 publications

References 45 publications

tRNA His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G −1 addition

tRNA His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G −1 addition

Function of the Extra 5‘-Phosphate Carried by Histidine tRNA

Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae

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Identity elements ofSaccharomyces cerevisiaetRNA^His

tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition

tRNA ^His guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G ₋₁ addition