Blaise M, Becker H D, Keith G, Cambillau C, Lapointe J, Giege R, Kern D
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon Journal Article
In: Nucleic Acids Res, vol. 32, no. 9, pp. 2768-2775, 2004, ISBN: 15150343, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN
@article{,
title = {A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon},
author = {M Blaise and H D Becker and G Keith and C Cambillau and J Lapointe and R Giege and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15150343},
isbn = {15150343},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {9},
pages = {2768-2775},
abstract = {Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying enzyme that evidently glutamylates the queuosine residue, a modified nucleoside at the wobble position of the tRNA(Asp) QUC anticodon. This conclusion is supported by a variety of biochemical data and by the inability of the enzyme to glutamylate tRNA(Asp) isolated from an E.coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine. Structural mimicry between the tRNA(Asp) anticodon stem and the tRNA(Glu) amino acid acceptor stem in prokaryotes encoding YadB proteins indicates that the function of these tRNA modifying enzymes, which we rename glutamyl-Q tRNA(Asp) synthetases, is conserved among prokaryotes.},
note = {1362-4962
Journal Article},
keywords = {Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Przykorska A, el Adlouni C, Keith G, Szarkowski J W, Dirheimer G
Structural specificity of Rn nuclease I as probed on yeast tRNA(Phe) and tRNA(Asp) Journal Article
In: Nucleic Acids Res, vol. 20, no. 4, pp. 659-663, 1992, ISBN: 1542562, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Asp/chemistry/genetics/*metabolism RNA, Base Composition Base Sequence Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't Yeasts/genetics, Pancreatic/*metabolism Secale cereale Substrate Specificity Support, Phe/chemistry/genetics/*metabolism Ribonuclease, Transfer, Unité ARN
@article{,
title = {Structural specificity of Rn nuclease I as probed on yeast tRNA(Phe) and tRNA(Asp)},
author = {A Przykorska and C el Adlouni and G Keith and J W Szarkowski and G Dirheimer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1542562},
isbn = {1542562},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {4},
pages = {659-663},
abstract = {A single-strand-specific nuclease from rye germ (Rn nuclease I) was characterized as a tool for secondary and tertiary structure investigation of RNAs. To test the procedure, yeast tRNA(Phe) and tRNA(Asp) for which the tertiary structures are known, as well as the 3'-half of tRNA(Asp) were used as substrates. In tRNA(Phe) the nuclease introduced main primary cuts at positions U33 and A35 of the anticodon loop and G18 and G19 of the D loop. No primary cuts were observed within the double stranded stems. In tRNA(Asp) the main cuts occurred at positions U33, G34, U35, C36 of the anticodon loop and G18 and C20:1 positions in the D loop. No cuts were observed in the T loop in intact tRNA(Asp) but strong primary cleavages occurred at positions psi 55, C56, A57 within that loop in the absence of the tertiary interactions between T and D loops (use of 3'-half tRNA(Asp)). These results show that Rn nuclease I is specific for exposed single-stranded regions.},
note = {0305-1048
Journal Article},
keywords = {Asp/chemistry/genetics/*metabolism RNA, Base Composition Base Sequence Molecular Sequence Data Nucleic Acid Conformation RNA, Non-U.S. Gov't Yeasts/genetics, Pancreatic/*metabolism Secale cereale Substrate Specificity Support, Phe/chemistry/genetics/*metabolism Ribonuclease, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}