Publications
2008
Kondo J, Westhof E
The bacterial and mitochondrial ribosomal A-site molecular switches possess different conformational substates Article de journal
Dans: Nucleic Acids Res, vol. 36, no. 8, p. 2654-2666, 2008, ISBN: 18346970, (1362-4962 (Electronic) Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Bacterial/*chemistry RNA, Crystallography, Messenger/chemistry RNA, Molecular Nucleic Acid Conformation Point Mutation RNA/*chemistry/genetics RNA, Ribosomal/*chemistry RNA, Transfer/chemistry, Unité ARN, WESTHOF, WESTHOF Crystallography, X-Ray Hearing Loss/genetics Humans Models
@article{,
title = {The bacterial and mitochondrial ribosomal A-site molecular switches possess different conformational substates},
author = {J Kondo and E Westhof},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18346970},
isbn = {18346970},
year = {2008},
date = {2008-01-01},
journal = {Nucleic Acids Res},
volume = {36},
number = {8},
pages = {2654-2666},
abstract = {The A site of the small ribosomal subunit participates in the fidelity of decoding by switching between two states, a resting 'off' state and an active decoding 'on' state. Eight crystal structures of RNA duplexes containing two minimal decoding A sites of the Homo sapiens mitochondrial wild-type, the A1555G mutant or bacteria have been solved. The resting 'off' state of the mitochondrial wild-type A site is surprisingly different from that of the bacterial A site. The mitochondrial A1555G mutant has two types of the 'off' states; one is similar to the mitochondrial wild-type 'off' state and the other is similar to the bacterial 'off' state. Our present results indicate that the dynamics of the A site in bacteria and mitochondria are different, a property probably related to the small number of tRNAs used for decoding in mitochondria. Based on these structures, we propose a hypothesis for the molecular mechanism of non-syndromic hearing loss due to the mitochondrial A1555G mutation.},
note = {1362-4962 (Electronic)
Journal Article},
keywords = {Bacterial/*chemistry RNA, Crystallography, Messenger/chemistry RNA, Molecular Nucleic Acid Conformation Point Mutation RNA/*chemistry/genetics RNA, Ribosomal/*chemistry RNA, Transfer/chemistry, Unité ARN, WESTHOF, WESTHOF Crystallography, X-Ray Hearing Loss/genetics Humans Models},
pubstate = {published},
tppubtype = {article}
}
1997
Wilhelm M., Heyman T., Friant S., Wilhelm F. X.
Heterogeneous terminal structure of Ty1 and Ty3 reverse transcripts Article de journal
Dans: Nucleic Acids Res, vol. 25, no. 11, p. 2161-6, 1997, (0305-1048 Journal Article).
Résumé | BibTeX | Étiquettes: *Nucleic, *Transcription, Acid, Calf, Chain, Conformation, DNA, Fungal/*chemistry/metabolism, Genetic, Gov't, H, Hybridization, Non-U.S., Nucleic, Plasmids/chemistry/genetics/metabolism, Polymerase, Reaction, Replication, Retroelements/*genetics, Ribonuclease, RNA, Support, Thymus/metabolism, Transfer/chemistry
@article{,
title = {Heterogeneous terminal structure of Ty1 and Ty3 reverse transcripts},
author = { M. Wilhelm and T. Heyman and S. Friant and F. X. Wilhelm},
year = {1997},
date = {1997-01-01},
journal = {Nucleic Acids Res},
volume = {25},
number = {11},
pages = {2161-6},
abstract = {A specific terminal structure of preintegrative DNA is required for transposition of retroviruses and LTR-retrotransposons. We have used an anchored PCR technique to map the 3'ends of DNA intermediates synthesized inside yeast Ty1 and Ty3 retrotransposon virus-like particles. We find that, unlike retroviruses, Ty1 replicated DNA does not have two extra base pairs at its 3'ends. In contrast some Ty3 preintegrative DNA molecules have two extra nucleotides at the 3'end of upstream and downstream long terminal repeats. Moreover we find that some molecules of replicated Ty3 DNA have more than two extra nucleotides at the 3'end of the upstream LTR. This observation could be accounted for by imprecise RNAse H cutting of the PPT sequence. The site of Ty1 and Ty3 plus-strand strong-stop DNA termination was also examined. Our results confirm that the prominent Ty1 and Ty3 plus-strand strong-stop molecules harbor 12 tRNA templated bases but also show that some Ty1 and Ty3 plus-strand strong-stop DNA molecules harbor less tRNA templated bases. We propose that these less than full length plus-strand molecules could be active intermediates in Ty retrotransposon replication.},
note = {0305-1048
Journal Article},
keywords = {*Nucleic, *Transcription, Acid, Calf, Chain, Conformation, DNA, Fungal/*chemistry/metabolism, Genetic, Gov't, H, Hybridization, Non-U.S., Nucleic, Plasmids/chemistry/genetics/metabolism, Polymerase, Reaction, Replication, Retroelements/*genetics, Ribonuclease, RNA, Support, Thymus/metabolism, Transfer/chemistry},
pubstate = {published},
tppubtype = {article}
}
1995
Keith G.
Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography Article de journal
Dans: Biochimie, vol. 77, no. 1-2, p. 142-4, 1995, (0300-9084 Journal Article).
BibTeX | Étiquettes: *Chromatography, Layer, Purines/chemistry, Pyrimidines/chemistry, Ribonucleases/metabolism, Ribonucleotides/*chemistry, RNA, Thin, Transfer/chemistry
@article{,
title = {Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography},
author = { G. Keith},
year = {1995},
date = {1995-01-01},
journal = {Biochimie},
volume = {77},
number = {1-2},
pages = {142-4},
note = {0300-9084
Journal Article},
keywords = {*Chromatography, Layer, Purines/chemistry, Pyrimidines/chemistry, Ribonucleases/metabolism, Ribonucleotides/*chemistry, RNA, Thin, Transfer/chemistry},
pubstate = {published},
tppubtype = {article}
}