Structural features required for the binding of tRNA<sup>Trp</sup>to avian myeloblastosis virus reverse transcriptase

Hu, James C.; Dahlberg, James E.

doi:10.1093/nar/11.14.4823

Cited by 18 publications

(14 citation statements)

References 36 publications

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“…Two types of evidences arise from the present study: (i) AMV reverse transcriptase interacts with the anticodon stem, the 3' side of the D arm and the 5' side of the T* stem of beef tRNATrp. The present data agree with previous results ( 9,39). Thus, the existence of protection in the anticodon stem region was shown by UV crosslinking experiments (7).…”

Section: Discussionsupporting

confidence: 94%

“…By affinity labelling of avian reverse transcriptase by periodate oxidated tRNATrP, the CCA end of tRNA was found covalently linked to the a subunit of reverse transcriptase which is the catalytic core of the polymerase (8). Recently it was shown that loop IV of tRNATrp containing the unusual sequence GpiC was important in binding to reverse transcri ptase (9).…”

Section: Introductionmentioning

confidence: 99%

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Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases

et al. 1984

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The interactions between beef tRNATrp with avian myeloblastosis reverse transcriptase have been studied by statistical chemical modifications of phosphate (ethylnitrosourea) and cytidine (dimethyl sulfate) residues, as well as by digestion of complexed tRNA by Cobra venom nuclease and Neurospora crassa endonuclease. Results with nucleases and chemicals show that reverse transcriptase interacts preferentially with the D arm, the anticodon stem and the T psi stem. All these regions are located in the outside of the L-shaped structure of tRNA. This domain of interaction is different to that reported previously in the complex of beef tRNA with the cognate aminoacyl-tRNA synthetase (M. Garret et al.; Eur. J. Biochem. In press). Avian reverse transcriptase destabilizes the region of tRNA where most of the tertiary interactions maintaining the structure of tRNA are located.

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Section: Discussionsupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases

et al. 1984

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“…However, it is not yet clear how RT specifically recognizes its cognate primer. Early experiments by Hu and Dahlberg (9) suggested that a fragment of tRNA' rp which retains the TipC loop and the acceptor stem was bound by AMV RT with about 80% of the efficiency of an intact tRNATrP. Barat et al (4) have reported that HIV-1 RT interacts with its cognate primer (tRNALYS) by virtue of specific interactions with the anticodon stem-loop.…”

Section: Pbsmentioning

confidence: 99%

A specific orientation of RNA secondary structures is required for initiation of reverse transcription

Aiyar

Leis

1994

J Virol

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611tRNATrP and the U5 sequences lying between the stem structures is necessary for efficient initiation of reverse transcription by avian sarcoma/leukosis virus reverse transcriptase (RT). An in vitro reconstituted system was used to demonstrate that stimulation of reverse transcription by the U5 RNA-TtiC interactions depends on both the U5-leader and U5-IR stem structures (1). In the present study, we show that the non-base-paired sequences between the various RNA secondary structures are also important for efficient reverse transcription, most probably by maintaining the duplex regions at a specific distance or orientation with respect to each other.

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“…The 2-fold difference in activity between beef and rabbit liver tR.NATrp may only be due to differences in the methods of preparation and storage of the two tRNAs since the sequence of tR-NATrp is largely conserved in avian and mammalian cells (8)(9)(10).…”

Section: Resultsmentioning

confidence: 99%

tRNATrp as cofactor of gelonin, a ribosome‐inactivating protein with RNA‐N‐glycosidase activity features required for the cofactor activity

et al. 1996

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SUMMARY. Purified beef and rabbit liver tRNATrP, but not yeast tRNATrp, increase the in vitro inactivation of eukaryotic ribosomes by gelonin, a ribosome-inactivating protein with RNA-Nglycosidase activity on 28S rRNA. Aminoacylation and stepwise trimming of the Y-end of bovine tRNATrp affect the cofactor activity, the most active species being that shortened by the last two nucleotides. ATP only moderately increases the activity of purified mammalian tRNATrp and in this increase the cognate aminoacyl-tRNA synthetase apparently has no role. Mobility shift experiments indicate that bovine tRNATrp binds both to ribosomes and to gelonin and favours the dissociation of gelonin from ribosomes. Depurination of isolated ribosomes by gelonin, the ribosome-inactivating protein (RIP) fromGelonium multiflorum with KNA-N-glycosidase activity on 28S rRNA, occurs at a very low rate unless ATP and macromolecular cofactors from a post-ribosomal supernatant are also present (1). In rat liver post-ribosomal supernatant one of the cofactors responsible for the up-regulation of gelonin is present in the tR_NA fraction isolated by Fast Flow Q-Sepharose chromatography (2). Sequential polyacrylamide gel electrophoresis of the tR_NA fraction led to the identification of the active cofactor in a tRNA about 70-nt long showing a high level of similarity with bovine tRNATrp (3). In this previous preparation, the tR_NA Trp obtained consisted of a mixture of two species lacking, respectively, one or two nucleotides at the CCA Y-end.Two cellular functions are well established for animal tKNATrp: its participation in protein biosynthesis and its role in the initiation of DNA synthesis by avian retroviruses (4). In these two roles the features of the tKNATrp molecule involved in the recognition, respectively, by the cognate tryptophanyl-tKNA synthetase (5) and by the viral reverse transoriptase (6-9) have been extensively studied.

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Structural features required for the binding of tRNA^Trpto avian myeloblastosis virus reverse transcriptase

Cited by 18 publications

References 36 publications

Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases

Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases

A specific orientation of RNA secondary structures is required for initiation of reverse transcription

tRNATrp as cofactor of gelonin, a ribosome‐inactivating protein with RNA‐N‐glycosidase activity features required for the cofactor activity

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Structural features required for the binding of tRNATrpto avian myeloblastosis virus reverse transcriptase

Cited by 18 publications

References 36 publications

Interactions between avian myeloblastosis reverse transcriptase and tRNATrp. Mapping of complexed tRNA with chemicals and nucleases

Interactions between avian myeloblastosis reverse transcriptase and tRNATrp. Mapping of complexed tRNA with chemicals and nucleases

A specific orientation of RNA secondary structures is required for initiation of reverse transcription

tRNATrp as cofactor of gelonin, a ribosome‐inactivating protein with RNA‐N‐glycosidase activity features required for the cofactor activity

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Structural features required for the binding of tRNA^Trpto avian myeloblastosis virus reverse transcriptase

Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases

Interactions between avian myeloblastosis reverse transcriptase and tRNA^Trp. Mapping of complexed tRNA with chemicals and nucleases