Théobald-Dietrich A, Frugier M, Giege R, Rudinger-Thirion J
Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA Journal Article
In: Nucleic Acids Res, vol. 32, no. 3, pp. 1091-1096, 2004, ISBN: 14872064, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Anticodon/metabolism Base Sequence Lysine/*analogs & derivatives/*metabolism Lysine-tRNA Ligase/metabolism Methanosarcina barkeri/genetics Mitochondria/genetics Molecular Sequence Data Nucleic Acid Conformation Peptide Elongation Factor Tu/*metabolism RNA, Archaeal/chemistry/*metabolism RNA, FRUGIER, Non-U.S. Gov't Yeasts/enzymology, Ser/chemistry Selenocysteine/metabolism Support, Transfer, Transfer/chemistry/*metabolism RNA, Unité ARN
@article{,
title = {Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA},
author = {A Théobald-Dietrich and M Frugier and R Giege and J Rudinger-Thirion},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14872064},
isbn = {14872064},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {3},
pages = {1091-1096},
abstract = {The newly discovered tRNA(Pyl) is involved in specific incorporation of pyrrolysine in the active site of methylamine methyltransferases in the archaeon Methanosarcina barkeri. In solution probing experiments, a transcript derived from tRNA(Pyl) displays a secondary fold slightly different from the canonical cloverleaf and interestingly similar to that of bovine mitochondrial tRNA(Ser)(uga). Aminoacylation of tRNA(Pyl) transcript by a typical class II synthetase, LysRS from yeast, was possible when its amber anticodon CUA was mutated into a lysine UUU anticodon. Hydrolysis protection assays show that lysylated tRNA(Pyl) can be recognized by bacterial elongation factor. This indicates that no antideterminant sequence is present in the body of the tRNA(Pyl) transcript to prevent it from interacting with EF-Tu, in contrast with the otherwise functionally similar tRNA(Sec) that mediates selenocysteine incorporation.},
note = {1362-4962
Journal Article},
keywords = {Anticodon/metabolism Base Sequence Lysine/*analogs & derivatives/*metabolism Lysine-tRNA Ligase/metabolism Methanosarcina barkeri/genetics Mitochondria/genetics Molecular Sequence Data Nucleic Acid Conformation Peptide Elongation Factor Tu/*metabolism RNA, Archaeal/chemistry/*metabolism RNA, FRUGIER, Non-U.S. Gov't Yeasts/enzymology, Ser/chemistry Selenocysteine/metabolism Support, Transfer, Transfer/chemistry/*metabolism RNA, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Marquet R, Isel C, Ehresmann C, Ehresmann B
tRNAs as primer of reverse transcriptases Journal Article
In: Biochimie, vol. 77, no. 1-2, pp. 113-124, 1995, ISBN: 7541250, (0300-9084 Journal Article Review Review, Tutorial).
Abstract | Links | BibTeX | Tags: Binding Sites DNA Nucleotidylexotransferase/genetics/metabolism Hepadnaviridae/genetics Introns Plant Viruses/genetics Plasmids RNA/chemistry/*metabolism RNA, MARQUET, Non-U.S. Gov't, Transfer/chemistry/*metabolism RNA, Unité ARN, Viral/genetics/*metabolism RNA-Directed DNA Polymerase/*metabolism Retroelements/genetics Retroviridae/genetics Support
@article{,
title = {tRNAs as primer of reverse transcriptases},
author = {R Marquet and C Isel and C Ehresmann and B Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7541250},
isbn = {7541250},
year = {1995},
date = {1995-01-01},
journal = {Biochimie},
volume = {77},
number = {1-2},
pages = {113-124},
abstract = {Genetic elements coding for proteins that present amino acid identity with the conserved motifs of retroviral reverse transcriptases constitute the retroid family. With the exception of reverse transcriptases encoded by mitochondrial plasmids of Neurospora, all reverse transcriptases have an absolute requirement for a primer to initiate DNA synthesis. In retroviruses, plant pararetroviruses, and retrotransposons (transposons containing long terminal repeats), DNA synthesis is primed by specific tRNAs. All these retroelements contain a primer binding site presenting a Watson-Crick complementarity with the primer tRNA. The tRNAs most widely used as primers are tRNA(Trp), tRNA(Pro), tRNA(1,2Lys), tRNA(3Lys), tRNA(iMet). Other tRNAs such as tRNA(Gln), tRNA(Leu), tRNA(Ser), tRNA(Asn) and tRNA(Arg) are also occasionally used as primers. In the retroviruses and plant pararetroviruses, the primer binding site is complementary to the 3' end of the primer tRNA. In the case of retrotransposons, the primer binding site is either complementary to the 3' end or to an internal region of the primer tRNA. Additional interactions taking place between the primer tRNA and the retro-RNA outside of the primer binding site have been evidenced in the case of Rous sarcoma virus, human immunodeficiency virus type I, and yeast retrotransposon Ty1. A selective encapsidation of the primer tRNA, probably promoted by interactions with reverse transcriptase, occurs during the formation of virus or virus-like particles. Annealing of the primer tRNA to the primer binding site appears to be mediated by reverse transcriptase and/or the nucleocapsid protein. Modified nucleosides of the primer tRNA have been shown to be important for replication of the primer binding site, encapsidation of the primer (in the case of Rous sarcoma virus), and interaction with the genomic RNA (in the case of human immunodeficiency virus type I).},
note = {0300-9084
Journal Article
Review
Review, Tutorial},
keywords = {Binding Sites DNA Nucleotidylexotransferase/genetics/metabolism Hepadnaviridae/genetics Introns Plant Viruses/genetics Plasmids RNA/chemistry/*metabolism RNA, MARQUET, Non-U.S. Gov't, Transfer/chemistry/*metabolism RNA, Unité ARN, Viral/genetics/*metabolism RNA-Directed DNA Polymerase/*metabolism Retroelements/genetics Retroviridae/genetics Support},
pubstate = {published},
tppubtype = {article}
}