The nucleotide sequences of cytoplasmic methionine and valine tRNAs from mouse myeloma cells

Piper, Peter W.; Clark, Brian F. C.

doi:10.1016/0014-5793(74)80425-4

Cited by 27 publications

(14 citation statements)

References 14 publications

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“…Sb were similar to each other and to that of "spot 6" (7). This tRNA appears to be tRNA4Met based on its fingerprint and minor nucleotide analysis of its oligonucleotides (26,27). The 2-dimensional electrophoretic profile of the tRNA not bound by reverse transcriptase (Fig.…”

Section: Methodsmentioning

confidence: 99%

Specific binding of tryptophan transfer RNA to avian myeloblastosis virus RNA-dependent DNA polymerase (reverse transcriptase).

Panet¹,

Haseltine²,

Baltimore³

et al. 1975

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

113

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The ability of tryptophan tRNA (tRNATrP) to initiate reverse transcription of the 70S RNA of avian RNA tumor viruses suggested that the reverse transcriptase (RNAdependent DNA polymerase; deoxynucleosidetriphosphate: DNA deoxynucleotidyltransferase; EC 2.7.7.7) might have a specific binding site for the tRNA. A complex of tRNATrP and the avian myeloblastosis virus reverse transcriptase has been demonstrated using chromatography on Sephadex G-100 columns. Of all the chicken tRNA's, only tRNATrP and a tRNA4Met bind to the enzyme with high enough affinity to be selected from a mixture of the chicken cell tRNAs. The ability of tRNATIP to change the sedimentation rate of the enzyme indicates that tRNATrP is not binding to a contaminant in the enzyme preparation. Treatment of the enzyme with monospecific antibody to reverse transcriptase prevented binding of tRNA as well as inhibited the DNA polymerase activity of the enzyme. The ability of reverse transcriptase to utilize tRNATrP as a primer for DNA synthesis, therefore, appears to involve a highly specific site on the enzyme.In vitro synthesis of DNA by the DNA polymerase (deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase, EC 2.7.7.7) found in virions of RNA tumor viruses (reverse transcriptase) is a primer-dependent reaction (1, 2). When the "70S" RNA from virions is used as a template, a lowmolecular-weight RNA of the 70S complex acts as primer (3-5). For Rous sarcoma virus, this RNA has been shown to be identical to a cellular tryptophan tRNA (tRNATrP) that is called "spot 1 RNA" after separation by 2-dimensional gel electrophoresis (6-9). Such tRNATrP has been isolated from three sources: 70S RNA, free 4S RNA from virions of Rous sarcoma virus, and normal chicken embryo fibroblasts (4,5,8).Although other tRNAs are found associated with 70S RNA and as free 4S RNA in virions (10), 90% of the DNA molecules copied from 70S RNA have been shown to be initiated using tRNATrP as a primer (4). Part of its ability to act as primer may result from the tight association of tRNATrP with the 35S RNA subunits of the 70S RNA; of the 70S-associated tRNAs, tRNATrP requires the highest temperature for removal from the 35S RNA (4, 11). The tRNATrP also appears to be able to anneal back to 35S RNA (12, 13). The association of tRNATrP with 35S RNA, however, is not sufficient to explain its ability to act as primer for the reverse transcriptase because, in general, the enzyme uses DNA efficiently as primer but utilizes RNA primers poorly (1, 14). The apparent selectivity of reverse transcriptase for tRNATrP over other 70S-associated tRNAs and the poor rate of priming of reverse transcriptase by RNA homopolymers led us to investigate whether there might be a specific binding site on the reverse transcriptase for tRNATrP. (7), using 1-2 mCi of [32P]orthophosphate per ml of medium. After 48 hr of labeling, virus was harvested from the medium by centrifugation and RNA was extracted without further purification (7). Viral RNA was fractionated into 70S and "free" 4S RNA b...

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Section: Methodsmentioning

confidence: 99%

Specific binding of tryptophan transfer RNA to avian myeloblastosis virus RNA-dependent DNA polymerase (reverse transcriptase).

Panet¹,

Haseltine²,

Baltimore³

et al. 1975

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

113

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“…Because tRNA from prokaryotic cells contains 1 mol of ribothymidine per mol of tRNA, whereas that of eukaryotic cells contains less than molar amounts of ribothymidine (11)(12)(13)(14)(15)(16)(17)(18), our laboratory has been interested in elucidating the function of this modified nucleoside in highly purified mammalian tRNAs.…”

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confidence: 99%

Role of ribothymidine in mammalian tRNAPhe.

Roe¹,

Tsen²

1977

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

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We have previously reported that mammalian tRNAsPhe from various tissues contain different amounts of ribothymidine and that a uridine methylase from Escherichia coli can quantitatively convert these tRNAs to species that contain their full complement of ribothymidine at position 23 from the 3' terminus. The role of ribothymidine in mammalian tRNAs has now been investigated by studying the ability of several highly purified mammalian tRNAsPhe, differing only in their ribothymidine content, to support poly(U)directed poly (Phe) synthesis under various conditions. Our results indicate that the ribothymidine content of mammalian tRNAPhe can be corre-

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“…Similar considerations could apply to the methionine-specific tRNAs from yeast. A unique feature in tRNAy" is the occurrence of two pseudouridine residues in opposite positions at the base of the anticodon stem (c), which so far were only found in the eukaryotic non-initiator tRNAsM" [15,16]. This may be a further structural detail which is characteristic for non-initiating tRNAsMe'.…”

Section: Pmentioning

confidence: 99%

“…with tRNAy"' are the following: the dihydrouridine loop contains 8 instead of 7 nucleotides, there is no unusual dinucleotide(-A*pG*p) [2] in stem (e), loop (IV) has the 'normal' construction Tp$pCpGp instead of ApUpCpGp. It has been suggested [15], that the different sequences of loop (I) and loop (IV) as well as the differences in stems (a), (c) and (e) in the mammalian type tRNAMe' may be important in specifying which tRNA will function in initiation or elongation of protein synthesis. Similar considerations could apply to the methionine-specific tRNAs from yeast.…”

Section: Pmentioning

confidence: 99%

“…This may be a further structural detail which is characteristic for non-initiating tRNAsMe'. The non-initiator tRNAsM"' from yeast and mammals also display many other similarities : the anti-codon arms, the extra loops, the dihydrouridine loops, and the [15,16] T$C loops are nearly identical. Altogether five base pairs in the acceptor stem, in the dihydrouridine stem, and in the T$C stem and one base each at position 20 in the dihydrouridine loop and at position 59 in the T$C loop are different.…”

Section: Pmentioning

confidence: 99%

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The Primary Structure of a Non-initiating Methionine-Specific tRNA from Brewer's Yeast

Gruhl¹,

Feldmann²

1976

Eur J Biochem

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tRNA3Met, one of the non‐initiating methionine‐specific tRNAs in brewer's yeast was purified from bulk tRNA labelled with [32P]phosphate by two column chromatographic steps. The primary structure of this tRNA was determined by the usual fingerprinting technique. Analyses of the isolated nucleotides and oligonucleotides from digests with pancreatic and T1 ribonucleases were in good agreement and stated that tRNA3Met consists of 76 nucleotide residues including 13 minor nucleotides. Overlaps from which the complete sequence could be deduced were derived from the analyses of 15 fragments obtained by partial digestion with T1 ribonuclease.

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The nucleotide sequences of cytoplasmic methionine and valine tRNAs from mouse myeloma cells

Cited by 27 publications

References 14 publications

Specific binding of tryptophan transfer RNA to avian myeloblastosis virus RNA-dependent DNA polymerase (reverse transcriptase).

Specific binding of tryptophan transfer RNA to avian myeloblastosis virus RNA-dependent DNA polymerase (reverse transcriptase).

Role of ribothymidine in mammalian tRNAPhe.

The Primary Structure of a Non-initiating Methionine-Specific tRNA from Brewer's Yeast

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