Transfer RNA Activities of Rous Sarcoma and Rous Associated Viruses

Wang, S.; Kothari, R. M.; Taylor, Milton W.; Hung, Paul P.

doi:10.1038/newbio242133a0

Cited by 35 publications

(38 citation statements)

References 23 publications

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“…molecules serving. as primers for reverse transcription are cOlnplexedwith a speciftc site in the virion RNA ofretrovirusf;ls (Randerath et al, 1971;Rosenthai and Zamechnik, 1973;Wang et al;. Firm binding of host leucine tRNA toMS2 virions has also been demonstrated (DiNatale and Eilat, 1976).…”

Section: Introductionmentioning

confidence: 99%

Aminoacylation of barley stripe mosaic virus RNA: Polyadenylate-containing RNA has a 3′-terminal tyrosine-accepting structure

Agranovsky¹,

Dolja

Gorbulev³

et al. 1981

Virology

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Barley stripe monie virus (BSMV) RNA whieb was previously reported to eontain poly(A) sequences (Agranovsky et al., 1978) ean be specifically esterified with tyrosine in vitro in the presence of an aminoacyl-tRNA syntbetase fraction from wheat embryos. All the tbree RNA components of tbe BSMV strain with a tbree-component genome (Norwieh) and botb RNA eomponents of a two-eomponent strain (Russian) can be tyrosylated. The poly(A)-containing (bound 10 oligo(dT)-ceUulose) and poly(A)-defieient (not bound 10 oligo(dT)-cellulose) fractions of BSMV RNA displaya similar amino acidaccepting ability. The nueleotide sequenee whieb aceepts tyrosine is coupled with the intact genomie polyadenylated BSMV RNA. The viral RNA isolated after suerose density gradient centrifugation under drastie denaturing conditions retains its aminoaeylating activity, whieb suggests that this aetivity is not due 10 tbe presence in a BSMV RNA preparation of a tyrosine tRNA associated witb BSMV RNA. Inhibition of aminoaeylation of tbe S'-oxidized (treated witb sodium metaperiodate) BSMV RNA suggests that the tyrosine-accepting strueture is loca1ized at the S' terminus of BSMV RNA molecules. It is sbown that segments of different lengths obtained upon random fragmentation ean be tyrosylated. The S'-terminal (tyrosine-accepting) poly(At segments ean be i80lated. The shortest segments of viral RNA eapable of beini aminoacylated [i.e .. containing both tRNA-like strueture and poly(A)] consists of approximately 150-200 nueleotides. The analysis of the oligonucleotides derived from individual BSMV RNA eomponents labeled with l2p at the S' end revealed two types of S'-terminal sequenees different from poly(A). It is suggested that a poly(A) sequence is intercalated between a S'-terminal tyrosineaccepting strueture and the S'-terminal portion of poly(At BSMV RNA.

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Section: Introductionmentioning

confidence: 99%

Aminoacylation of barley stripe mosaic virus RNA: Polyadenylate-containing RNA has a 3′-terminal tyrosine-accepting structure

Agranovsky¹,

Dolja

Gorbulev³

et al. 1981

Virology

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“…In the absence of this RNA primer molecule the template activity of RSV RNA is no better than that of other natural RNA molecules (14,17), suggesting that the preference exhibited by the RNA-directed DNA polymerase for oncornavirus 70S RNA as template is a special feature of the RNA and not a property of the enzyme. Although no virus-specific functions have previously been assigned to any of the other low molecular weight RNA species associated with virions of RNA tumor viruses, many of the virion-associated tRNA species appear to be cellular in origin and selectively incorporated into the virus particle during budding of the virus from the cell membrane (3,(7)(8)(9)(10)(11) (21). These results indicate that the 4S RNA primer molecule required by the RSV RNA-directed DNA polymerase for the initiation of DNA synthesis in vitro is present in normal, uninfected cells, and is in all likelihood a cell-specified molecule.…”

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confidence: 99%

“…The low-molecular-weight population includes 7S, 5S, and 4S RNA and is generally referred to as RSV-free (not associated with 70S RNA) RNA (1)(2)(3)(4)(5)(6). The free 4S RNA exhibits structural features of transfer RNA (tRNA) and can be acylated with amino acids (3,(5)(6)(7)(8)(9)(10)(11). RSV 70S RNA is segmented in nature, containing three to four high-molecular-weight 30-35S RNA subunits (1) and several low-molecular-weight species.…”

mentioning

confidence: 99%

RNA-directed DNA synthesis by the DNA polymerase of Rous sarcoma virus: structural and functional identification of 4S primer RNA in uninfected cells.

Faras¹,

Dibble²

1975

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

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The RNA-directed DNA Virions of Rous sarcoma virus (RSV) contain two major size classes of RNA: 70S RNA presumed to be the viral genome, and a low-molecular-weight population consisting of a number of discrete RNA species. The low-molecular-weight population includes 7S, 5S, and 4S RNA and is generally referred to as RSV-free (not associated with 70S RNA) RNA (1-6). The free 4S RNA exhibits structural features of transfer RNA (tRNA) and can be acylated with amino acids (3, 5-11). RSV 70S RNA is segmented in nature, containing three to four high-molecular-weight 30-35S RNA subunits (1) and several low-molecular-weight species. This latter group includes 7S, 5S, and 4S RNA and is referred to as 70S-associated (70S-a) RNA (5,(12)(13)(14).Transcription in vitro of the 70S RNA genome of avian RNA tumor viruses by the RNA-directed DNA polymerase is initiated by covalent attachment of DNA to the 3' terminus of an RNA primer molecule (15-17). We have recently identified the RNA primer molecule as a low-molecularweight RNA species, 75 nucleotides in length, exhibiting structural features analogous to those of tRNA (18)(19)(20). This molecule appears to be the principal primer utilized by the RSV DNA polymerase, since its removal from 70S RNA results in the loss of 80-90% of the template activity of the 70S RNA complex (14, 17). In the absence of this RNA primer molecule the template activity of RSV RNA is no better than that of other natural RNA molecules (14, 17), suggesting that the preference exhibited by the RNA-directed DNA polymerase for oncornavirus 70S RNA as template is a special feature of the RNA and not a property of the enzyme. Although no virus-specific functions have previously been assigned to any of the other low molecular weight RNA species associated with virions of RNA tumor viruses, many of the virion-associated tRNA species appear to be cellular in origin and selectively incorporated into the virus particle during budding of the virus from the cell membrane (3, 7-11). It was of considerable interest, therefore, to determine whether the RNA primer molecule was a normal constituent of uninfected cells, or a virus-specified or virus-induced molecule.In

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“…Avian RNA tumor viruses such as avian myeloblastosis virus (AMV), Rous associated virus-1, and Rous sarcoma virus contain a population of functional transfer RNA (tRNA) molecules that differs from the total tRNA of their host cells, both in range and in level of aminoacid-accepting activity (1)(2)(3)(4)(5). It has been established that this RNA is neither a contaminant of the preparation nor a degradation product, but is an integral part of the virion (4-6), In addition purified virions of AMV contain aminoacyl-tRNA synthetase activities (7,8) and a specific tRNA methylase (9), A comparison of the base composition of AMV tRNA with that of both normal and transformed host cells indicates that the viral RNA contains all the minor bases that are present in host tRNA.…”

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confidence: 99%

Methionine Transfer Ribonucleic Acids of Avian Myeloblastosis Virus

Elder

Smith

1973

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

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Chick-embryo cells contain four isoaccepting species of methionine transfer RNA (I-IV). One species (I) is the initiator, tRNA'et, and the others (II, III, and IV) are the donors of internal methionyl residues (tRNAmet). Over 85% of the tRNAMet in purified avian myeloblastosis virus consists of one tRNAmt species, which resembles host-cell tRNAMet IV with respect to chromatographic properties on Avian RNA tumor viruses such as avian myeloblastosis virus (AMV), Rous associated virus-1, and Rous sarcoma virus contain a population of functional transfer RNA (tRNA) molecules that differs from the total tRNA of their host cells, both in range and in level of aminoacid-accepting activity (1-5). It has been established that this RNA is neither a contaminant of the preparation nor a degradation product, but is an integral part of the virion (4-6), In addition purified virions of AMV contain aminoacyl-tRNA synthetase activities (7, 8) and a specific tRNA methylase (9), A comparison of the base composition of AMV tRNA with that of both normal and transformed host cells indicates that the viral RNA contains all the minor bases that are present in host tRNA. There is no evidence for additional modifications in the viral RNA, but the distribution of certain minor bases is altered (3). Although there is no direct evidence as to the origin of viral tRNA, it is probable that a selection of a limited population of host-cell molecules takes place to provide the virion tRNA. Alternatively, the tRNAs found in the virus could be unique to the virus, or contain specific modifications of host-cell tRNAs. The experiments described here were done in an attempt to detect unique viral tRNAs, if they exist. Reversed-phase chromatography on RPC-5 absorbent of AMV tRNA charged with single aminoacids reveals that the virus contains particular isoaccepting species of the corresponding host-cell tRNA. In some cases, the ratio of different isoaccepting species is altered (Elder, unpublished). Thus, whereas chick cells contain four peaks of methionyl-tRNA, both AMV and Rous associated virus-i have a single predominating methionyl-tRNA that is chromatographically similar to one of the host tRNAMet species (2). In view of the degree of selectivity and the unique role of methionyl-tRNA in initiation of protein synthesis (10), it was important to determine whether the tRNAMet present in the virus was somehow involved in initiation of viral protein synthesis.Eukaryotic cells contain two classes of methionine-accepting tRNA, tRNAmet and tRNAmet (10). Met-tRNAm, in common with all aminoacyl-tRNAs, donates its amino acid into internal positions of peptides, whereas Met-tRNAf is the initiator tRNA. A distinguishing Teature of the initiator is thatMet-tRNAf donates methionine exclusively into the Nterminal position of newly synthesized proteins. This property results from its specific interaction with initiation factors (11), andj inability to form a stable complex with elongation factor I (12), both of which imply that the structure of tRNAIet ha...

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Transfer RNA Activities of Rous Sarcoma and Rous Associated Viruses

Cited by 35 publications

References 23 publications

Aminoacylation of barley stripe mosaic virus RNA: Polyadenylate-containing RNA has a 3′-terminal tyrosine-accepting structure

Aminoacylation of barley stripe mosaic virus RNA: Polyadenylate-containing RNA has a 3′-terminal tyrosine-accepting structure

RNA-directed DNA synthesis by the DNA polymerase of Rous sarcoma virus: structural and functional identification of 4S primer RNA in uninfected cells.

Methionine Transfer Ribonucleic Acids of Avian Myeloblastosis Virus

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