Related ArticlesNMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.
Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11467-71
Authors: Puglisi EV, Puglisi JD, Williamson JR, RajBhandary UL
An important step in initiation of protein synthesis in Escherichia coli is the specific formylation of the initiator methionyl-tRNA (Met-tRNA) by Met-tRNA transformylase. The determinants 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 microhelices, which correspond to the acceptor stem of mutants of E. coli initiator 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 transformylase, whereas the other one is a much better substrate. We show that one microhelix forms a structure in which its 3'-ACCA sequence extends the stacking 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 close proximity to G1. These results highlight 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 transformylase.
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200189u/aop/images/medium/bi-2011-00189u_0010.gif
Biochemistry
DOI: 10.1021/bi200189u
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04-13-2011 01:25 PM
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
Biochemistry. 2011 Mar 25;
Authors: Paukstelis PJ, Chari N, Lambowitz AM, Hoffman DW
The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNATyr and are structure-stabilizing splicing cofactors for group I introns. Studies with the Neurospora...
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....
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12-15-2010 12:03 PM
[NMR paper] The hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding an
The hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding and antimetastatic activity: an NMR evaluation.
Related Articles The hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding and antimetastatic activity: an NMR evaluation.
J Inorg Biochem. 2004 Feb;98(2):402-12
Authors: Bacac M, Hotze AC, van der Schilden K, Haasnoot JG, Pacor S, Alessio E, Sava G, Reedijk J
The coordination of the antimetastatic agent NAMI-A, , (Him=imidazole; dmso=dimethyl sulfoxide), to the DNA model base...
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11-24-2010 09:25 PM
[NMR paper] NMR structure of the 3' stem-loop from human U4 snRNA.
NMR structure of the 3' stem-loop from human U4 snRNA.
Related Articles NMR structure of the 3' stem-loop from human U4 snRNA.
Nucleic Acids Res. 2002 Oct 15;30(20):4371-9
Authors: Comolli LR, Ulyanov NB, Soto AM, Marky LA, James TL, Gmeiner WH
The NMR structure of the 3' stem-loop (3'SL) from human U4 snRNA was determined to gain insight into the structural basis for conservation of this stem-loop sequence from vertebrates. 3'SL sequences from human, rat, mouse and chicken U4 snRNA each consist of a 7 bp stem capped by a UACG tetraloop. No...
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11-24-2010 08:58 PM
[NMR paper] Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid pr
Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
Related Articles Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
J Mol Biol. 2001 Feb 23;306(3):443-54
Authors: Tisné C, Roques BP, Dardel F
Reverse transcription of HIV-1 viral RNA uses human tRNA(Lys)3 as a primer. Recombinant tRNA(Lys)3 was previously overexpressed in Escherichia coli, 15N-labelled and purified for NMR studies. It was shown to be functional for priming of HIV-1 reverse transcription. Using...
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11-19-2010 08:32 PM
[NMR paper] Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase
Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression Host Scott Ross was helpful in conducting the 1D TOCSY NMR experiments and Pratip Bhattachary is thanked for assistance in other NMR experiments. We are grateful to Yves Mechulam for a sample of plasmid pBSM547W305F and to Hieronim Jakubowski of UMDNJ-New Jersey Medical School, Newark, New Jersey, for plasmid pGG3. K.L.K. thanks the U.S. Department of Defense for a National Defense Science and Engineering Graduate Fellowship. This work was supported by grants from the...