Interactions between avian myeloblastosis reverse transcriptase and tRNA<sup>Trp</sup>. Mapping of complexed tRNA with chemicals and nucleases

Garret, Maurice; Romby, Pascale; Giegé, Richard; Litvak, Simón

doi:10.1093/nar/12.5.2259

Cited by 30 publications

(12 citation statements)

References 37 publications

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“…Furthermore, we have delineated a region in this tRNA, the anti-codon domain, which is most likely the contact site recognized by HIV-1 RT. A similar pattern of tRNA recognition has been reported for AMV RT, which binds primer tRNAT'p (Araya et al, 1980;Garret et al, 1984). An interesting observation from Figure 5 is that a similarly sized TI RNase generated oligoribonucleotide can be obtained with an HIV-1 RT-tRNATrp complex, albeit in extremely low amounts.…”

Section: Discussionsupporting

confidence: 77%

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

et al. 1989

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The virion cores of the replication competent type 1 human immunodeficiency virus (HIV‐1), a retrovirus, contain and RNA genome associated with nucleocapsid (NC) and reverse transcriptase (RT p66/p51) molecules. In vitro reconstructions of these complexes with purified components show that NC is required for efficient annealing of the primer tRNALys,3. In the absence of NC, HIV‐1 RT is unable to retrotranscribe the viral RNA template from the tRNA primer. We demonstrate that the HIV‐1 RT p66/p51 specifically binds to its cognate primer tRNALys,3 even in the presence of a 100‐fold molar excess of other tRNAs. Cross‐linking analysis of this interaction locates the contact site to a region within the heavily modified anti‐codon domain of tRNALys,3.

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Section: Discussionsupporting

confidence: 77%

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

et al. 1989

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“…Diversity in tRNA structural properties allows these seminal macromolecules not only to be the actors of translation but also to have key functions in a growing number of other cellular events 3,5,7. They not only bind to unrelated partners such as cytochrome c143 or lipids,7 but their plasticity is such that they can cross membranes87 or become partly unfolded as is the case in initiation of retroviral reverse transcription 144. It is likely that new functions will still become highlighted.…”

Section: Discussionmentioning

confidence: 99%

Synthesis, Enzymatic Evaluation, and Docking Studies of Fluorogenic Caspase 8 Tetrapeptide Substrates

et al. 2009

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The synthesis, enzymatic evaluation, and molecular modeling studies of new fluorogenic tetrapeptide-based substrates selective for caspase 8, having the general structure Ac-IETD-AXX, are described. Various fluorescent reporter groups (AXX), i.e., 3- and 4-substituted coumarins and quinolin-2(1H)-ones were synthesized by von Pechmann condensation. They were subsequently coupled with the caspase-8-selective tetrapeptide Ac-IETD-OH under newly developed synthetic conditions to give the desired substrates in good yields and in high enantiomeric purity. Based on K(M) and V(max) values, the new compounds proved to be excellent substrates for recombinant human caspase 8. In contrast, the K(M) values for the same compounds as substrates for human caspase 3 were approximately 10-20-fold higher. Molecular modeling studies based on the X-ray crystal structures of both human caspases 3 and 8 revealed that there is sufficient room within both active sites to accommodate substrates with moderately bulky substituents in the 3- and 4-positions of the fluorogenic coumarins and quinolin-2(1H)-ones. Automated docking of the substrates into the active sites of both human caspases 3 and 8 with the program AutoDock 3 gave structures similar to the published crystallographic structures for the same tetrapeptide bound to caspase 8 in the form of an irreversible inhibitor. The calculated binding energies for the new substrates to either caspase 3 or 8 showed little difference between the substrates, consistent with the K(M) data. In addition, the calculated binding energies (DeltaG) to caspase 8 were considerably more negative than those to caspase 3, also consistent with the K(M) data. A possible molecular interaction that might explain the selectivity of the IETD tetrapeptide motif for caspase 8 over caspase 3 is discussed.

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

Cited by 30 publications

References 37 publications

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

Synthesis, Enzymatic Evaluation, and Docking Studies of Fluorogenic Caspase 8 Tetrapeptide Substrates

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

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

Cited by 30 publications

References 37 publications

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

Synthesis, Enzymatic Evaluation, and Docking Studies of Fluorogenic Caspase 8 Tetrapeptide Substrates

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

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