M3i

@article{,

title = {Strategy for RNA recognition by yeast histidyl-tRNA synthetase},

author = {J Rudinger and B Felden and C Florentz and R Giege},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9222493},

isbn = {9222493},

year  = {1997},

date = {1997-01-01},

journal = {Bioorg Med Chem},

volume = {5},

number = {6},

pages = {1001-1009},

abstract = {Histidine aminoacylation systems are of interest because of the structural diversity of the RNA substrates recognized by histidyl-tRNA synthetases. Among tRNAs participating in protein synthesis, those specific for histidine all share an additional residue at their 5'-extremities. On the other hand, tRNA-like domains at the 3'--termini of some plant viruses can also be charged by histidyl-tRNA synthetases, although they are not actors in protein synthesis. This is the case for the RNAs from tobacco mosaic virus and its satellite virus but also those of turnip yellow and brome mosaic viruses. All these RNAs have intricate foldings at their 3'-termini differing from that of canonical tRNAs and share a pseudoknotted domain which is the prerequisite for their folding into structures mimicking the overall L-shape of tRNAs. This paper gives an overview on tRNA identity and rationalizes the apparently contradictory structural and aminoacylation features of histidine-specific tRNAs and tRNA-like structures. The discussion mainly relies on histidylation data obtained with the yeast synthetase, but the conclusions are of a more universal nature. In canonical tRNA(His), the major histidine identity element is the 'minus' 1 residue, since its removal impairs histidylation and conversely its addition to a non-cognate tRNA(Asp) confers histidine identity to the transplanted molecule. Optimal expression of histidine identity depends on the chemical nature of the -1 residue and is further increased and/or modulated by the discriminator base N73 and by residues in the anticodon. In the viral tRNA-like domains, the major identity determinant -1 is mimicked by a residue from the single-stranded L1 regions of the different pseudoknots. The consequences of this mimicry for the function of minimalist RNAs derived from tRNA-like domains are discussed. The characteristics of the histidine systems illustrate well the view that the core of the amino acid accepting RNAs is a scaffold that allows proper presentation of identity nucleotides to their amino acid identity counterparts in the synthetase and that different types of scaffoldings are possible.},

note = {0968-0896 

Journal Article 

Review 

Review, Tutorial},

keywords = {Amino Acyl/metabolism  RNA, Base Sequence  Histidine-tRNA Ligase/*metabolism  Molecular Sequence Data  RNA, FLORENTZ, Fungal/*metabolism  RNA, Non-U.S. Gov't, Transfer, Unité ARN, Viral/metabolism  Saccharomyces cerevisiae/*enzymology  Substrate Specificity  Support},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Intron-dependent formation of pseudouridines in the anticodon of Saccharomyces cerevisiae minor tRNA(Ile)},

author = {Z Szweykowska-Kulinska and B Senger and G Keith and F Fasiolo and H Grosjean},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7925304},

isbn = {7925304},

year  = {1994},

date = {1994-01-01},

journal = {EMBO J},

volume = {13},

number = {19},

pages = {4636-4644},

abstract = {We have isolated and sequenced the minor species of tRNA(Ile) from Saccharomyces cerevisiae. This tRNA contains two unusual pseudouridines (psi s) in the first and third positions of the anticodon. As shown earlier by others, this tRNA derives from two genes having an identical 60 nt intron. We used in vitro procedures to study the structural requirements for the conversion of the anticodon uridines to psi 34 and psi 36. We show here that psi 34/psi 36 modifications require the presence of the pre-tRNA(Ile) intron but are not dependent upon the particular base at any single position of the anticodon. The conversion of U34 to psi 34 occurs independently from psi 36 synthesis and vice versa. However, psi 34 is not formed when the middle and the third anticodon bases of pre-tRNA(Ile) are both substituted to yield ochre anticodon UUA. This ochre pre-tRNA(Ile) mutant has the central anticodon uridine modified to psi 35 as is the case for S.cerevisiae SUP6 tyrosine-inserting ochre suppressor tRNA. In contrast, neither the first nor the third anticodon pseudouridine is formed, when the ochre (UUA) anticodon in the pre-tRNA(Tyr) is substituted with the isoleucine UAU anticodon. A synthetic mini-substrate consisting of the anticodon stem and loop and the wild-type intron of pre-tRNA(Ile) is sufficient to fully modify the anticodon U34 and U36 into psi s. This is the first example of the tRNA intron sequence, rather than the whole tRNA or pre-tRNA domain, being the main determinant of nucleoside modification.},

note = {0261-4189 

Journal Article},

keywords = {Anticodon/*metabolism  Base Sequence  Introns/*physiology  Molecular Sequence Data  Nucleic Acid Conformation  Pseudouridine/*biosynthesis  RNA Processing, Fungal/*metabolism  RNA, Ile/*metabolism  Saccharomyces cerevisiae/*genetics  Support, Non-U.S. Gov't, Post-Transcriptional/physiology  RNA, Transfer, Unité ARN},

pubstate = {published},

tppubtype = {article}

}