Nucleotide Sequence of N-Formyl-methionyl-transfer RNA

Dube, Shyam K.; Marcker, Kjeld A.; Clark, Brian F. C.; Cory, Suzanne

doi:10.1038/218232a0

Cited by 286 publications

(73 citation statements)

References 12 publications

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“…A nacystis t RNA Met is homogenous both with regard to nucleotide sequence and base modification, although the E. coli initiator is heterogenous in one position of the sequence [5].…”

Section: Resultsmentioning

confidence: 99%

“…The Anacystis tRNA Met is 77 nucleotides in length and contains five modified nucleotides: D, T, if, mVG and C m. Whereas 4-thiouridine occupies position 8 in b2 coli tRNA Met [5], no evidence for this modified nucleoside has been found in A nacystis even after isolation of the tRNA in the presence of thiosulfate [ 15 ]. A nacystis t RNA Met is homogenous both with regard to nucleotide sequence and base modification, although the E. coli initiator is heterogenous in one position of the sequence [5].…”

Section: Resultsmentioning

confidence: 99%

“…With the algal sequence presented here, three formylmethionine tRNA sequences from widely divergent prokaryotes are now available for comparison [5,8]. The three prokaryotic sequences have a non base-paired 5' terminal nucleotide.…”

Section: Discussionmentioning

confidence: 99%

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The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs

Ecarot-Charrier

Cedergren

1976

FEBS Letters

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“…A nacystis t RNA Met is homogenous both with regard to nucleotide sequence and base modification, although the E. coli initiator is heterogenous in one position of the sequence [5].…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs

Ecarot-Charrier

Cedergren

1976

FEBS Letters

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“…In addition, results of electron paramagnetic resonance studies on spinlabeled tRNAfmet (23), studies of the RNA ligase-catalyzed intramolecular joining of 3'-OH of tRNAfmet to the 5'-phosphate leading to its circularization (24), and fluorescence energy transfer studies (25) are in general consistent with a fold-back structure for the tRNA. The acceptor stem of tRNA~fet differs from the A19 variant only in that the former has a ClxA72 mismatch (26), whereas the latter has a G-C base pair at the corresponding position. Thus, the C1xA72 mismatch in tRNAAfmet favors the formation of a fold-back structure even when the discriminator base is A.…”

Section: Discussionmentioning

confidence: 99%

NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.

Puglisi

Williamson

et al. 1994

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

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An important step in initiation of protein synthesis in Escherichia col is the specific formylation of the initiator methionyl-tRNA (Met-tRNA) by Met-tRNA transformylase. The deterinants for formylation are clustered mostly in the acceptor stem of the initiator tRNA. Here we use NMR spectroscopy to characterize the conformation of two RNA microhelces, which correspond to the acceptor stem of mutants of E. coUi initator tRNA and which differ only at the position corresponding to the "discriminator base" in tRNAs.One of the mutant tRNAs is an extremely poor substrate for Met-tRNA trausformylase, whereas the other one is a much better substrate. We show that one microhelix forms a struchire in which its 3'-ACCA sequence extends the tacklng of the acceptor stem. The other microhelix forms a structure in which its 3'-UCCA sequence folds back such that the 3'-terminal A22 is in dose proximity to GI. These results highiight the importance of the discriminator base in determining tRNA conformation at the 3' end. They also suggest a correlation between tRNA structure at the 3' end and its recognition by Met-tRNA trandormylase.Protein synthesis in Escherichia coli is initiated with formylmethionyl-tRNA (tMet-tRNA). A crucial step in this process is the specific formylation of methionine attached to tRNAfmet by Met-tRNA transformylase (EC 2.1.2.9) (1, 2). We showed previously that the major determinants for formylation are clustered in the acceptor stem of tRNA (3). One of these determinants is a mismatch (as found in tRNAfmet) or a weak base pair at the end of the acceptor stem. tRNAs carrying the wild-type ClxA72 or virtually any other mismatch are good substrates, whereas those carrying stable base pairs such as ClG72 or GlFC72 are extremely poor substrates (4-6). These results suggest a requirement for nucleotides 1 and 72 to be unpaired during formylation.The strong negative effect of ClG72 or G1C72 base pairs on formylation can be compensated for by an additional mutation of A73, the discriminator base, which precedes the CCA sequence common to all tRNAs, to a pyrimidine such as U73 (4). For example, in contrast to the ClG72 mutant, which is a very poor substrate (V 1/K aPP down by a factor of495 compared to wild-type tRNA), the ClG72/U73 mutant is almost as good a substrate as wild-type tRNA (V./KIPP down only by a factor of 3.7). Similarly, compared to the G1*C72 mutant, the G1'C72/U73 mutant is a better substrate for Met-tRNA transformylase (V./KIPP down by a factor of 60, while the factor is 1035 for the G1-C72 mutant). On the basis of these results, we proposed that the discriminator base influences the stability of the terminal base pair in the acceptor stem and/or structure of tRNA at the 3' end (4, 6).In this paper, we use NMR spectroscopy (7) to study the effect of the discriminator base (8) on tRNA conformation at the 3' end. Two RNA oligonucleotides that correspond to variants of the acceptor stem of initiator tRNAfmet were designed for NMR study (Fig. 1A). These oligonucleotides contain the seven ...

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“…1 C), that all tRNAsMet belong to the class I type of &RNAs [20] with variations off 1 nucleotide in the D-loop (I) and that two out of the three postulated base triples [21], namely C13, G22, m'G46 and U8,A14, A21 remain constant in this group of tRNAs, while the third possible base triple could vary: A9,U12,A23 (tRNA@' in E. coli and yeast), G9,G12,C23 or m'G9, G12$23 in the initiator tRNAs, and A9,G12$23 (?) in tRNAyef ( y I m e oma).…”

Section: Recognition Sites and Evolutionary Aspectsmentioning

confidence: 99%

The primary structure of a non‐initiating methionine specific tRNA from brewer's yeast

Gruhl¹,

Feldmann²

1975

FEBS Letters

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Nucleotide Sequence of N-Formyl-methionyl-transfer RNA

Cited by 286 publications

References 12 publications

The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs

The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs

NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.

The primary structure of a non‐initiating methionine specific tRNA from brewer's yeast

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Nucleotide Sequence of N-Formyl-methionyl-transfer RNA

Cited by 286 publications

References 12 publications

The preliminary sequence of tRNAMetF from Anacystis nidulans compared with other initiator tRNAs

The preliminary sequence of tRNAMetF from Anacystis nidulans compared with other initiator tRNAs

NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.

The primary structure of a non‐initiating methionine specific tRNA from brewer's yeast

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The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs

The preliminary sequence of tRNA^Met_F from Anacystis nidulans compared with other initiator tRNAs