Publications
2003
Ennifar E, Walter P, Dumas P
A crystallographic study of the binding of 13 metal ions to two related RNA duplexes Article de journal
Dans: Nucleic Acids Res, vol. 31, no. 10, p. 2671-2682, 2003, ISBN: 12736317, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Base Sequence Binding Sites/genetics Binding, Competitive Cations, Divalent/chemistry/metabolism Cobalt/chemistry/metabolism Comparative Study Crystallization Crystallography, ENNIFAR, Molecular Nucleic Acid Heteroduplexes/*chemistry/genetics/metabolism Oligoribonucleotides/chemistry/genetics/metabolism Platinum Compounds/chemistry/metabolism RNA/*chemistry/genetics/metabolism Ruthenium Compounds/chemistry/metabolism Support, Non-U.S. Gov't, Unité ARN, X-Ray Gold Compounds/chemistry/metabolism Magnesium/chemistry/metabolism Metals/*chemistry/metabolism Models
@article{,
title = {A crystallographic study of the binding of 13 metal ions to two related RNA duplexes},
author = {E Ennifar and P Walter and P Dumas},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12736317},
isbn = {12736317},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {10},
pages = {2671-2682},
abstract = {Metal ions, and magnesium in particular, are known to be involved in RNA folding by stabilizing secondary and tertiary structures, and, as cofactors, in RNA enzymatic activity. We have conducted a systematic crystallographic analysis of cation binding to the duplex form of the HIV-1 RNA dimerization initiation site for the subtype-A and -B natural sequences. Eleven ions (K+, Pb2+, Mn2+, Ba2+, Ca2+, Cd2+, Sr2+, Zn2+, Co2+, Au3+ and Pt4+) and two hexammines [Co (NH3)6]3+ and [Ru (NH3)6]3+ were found to bind to the DIS duplex structure. Although the two sequences are very similar, strong differences were found in their cation binding properties. Divalent cations bind almost exclusively, as Mg2+, at 'Hoogsteen' sites of guanine residues, with a cation-dependent affinity for each site. Notably, a given cation can have very different affinities for a priori equivalent sites within the same molecule. Surprisingly, none of the two hexammines used were able to efficiently replace hexahydrated magnesium. Instead, [Co (NH3)4]3+ was seen bound by inner-sphere coordination to the RNA. This raises some questions about the practical use of [Co (NH3)6]3+ as a [Mg (H2O)6]2+ mimetic. Also very unexpected was the binding of the small Au3+ cation exactly between the Watson-Crick sites of a G-C base pair after an obligatory deprotonation of N1 of the guanine base. This extensive study of metal ion binding using X-ray crystallography significantly enriches our knowledge on the binding of middleweight or heavy metal ions to RNA, particularly compared with magnesium.},
note = {1362-4962
Journal Article},
keywords = {Base Sequence Binding Sites/genetics Binding, Competitive Cations, Divalent/chemistry/metabolism Cobalt/chemistry/metabolism Comparative Study Crystallization Crystallography, ENNIFAR, Molecular Nucleic Acid Heteroduplexes/*chemistry/genetics/metabolism Oligoribonucleotides/chemistry/genetics/metabolism Platinum Compounds/chemistry/metabolism RNA/*chemistry/genetics/metabolism Ruthenium Compounds/chemistry/metabolism Support, Non-U.S. Gov't, Unité ARN, X-Ray Gold Compounds/chemistry/metabolism Magnesium/chemistry/metabolism Metals/*chemistry/metabolism Models},
pubstate = {published},
tppubtype = {article}
}
2000
Moine H, Squires C L, Ehresmann B, Ehresmann C
In vivo selection of functional ribosomes with variations in the rRNA-binding site of Escherichia coli ribosomal protein S8: evolutionary implications Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 97, no. 2, p. 605-610, 2000, ISBN: 10639126, (0027-8424http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10639126 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/genetics/metabolism Recombinant Fusion Proteins/genetics/metabolism Ribosomal Proteins/genetics/*metabolism Ribosomes/genetics/*metabolism Spectinomycin/pharmacology Support, Base Sequence Binding Sites/genetics Binding, Competitive Cell Division/genetics Cloning, Microbial Escherichia coli/drug effects/*genetics/metabolism Evolution, Molecular Drug Resistance, Molecular Protein Binding RNA, P.H.S. Variation (Genetics), Ribosomal, Ribosomal/genetics/*metabolism RNA, U.S. Gov't, Unité ARN
@article{,
title = {In vivo selection of functional ribosomes with variations in the rRNA-binding site of Escherichia coli ribosomal protein S8: evolutionary implications},
author = {H Moine and C L Squires and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10639126},
isbn = {10639126},
year = {2000},
date = {2000-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {97},
number = {2},
pages = {605-610},
abstract = {The highly conserved nature of rRNA sequences throughout evolution allows these molecules to be used to build philogenic trees of different species. It is unknown whether the stability of specific interactions and structural features of rRNA reflects an optimal adaptation to a functional task or an evolutionary trap. In the work reported here, we have applied an in vivo selection strategy to demonstrate that unnatural sequences do work as a functional replacement of the highly conserved binding site of ribosomal protein S8. However, growth competition experiments performed between Escherichia coli isolates containing natural and unnatural S8-binding sites showed that the fate of each isolate depended on the growth condition. In exponentially growing cells, one unnatural variant was found to be equivalent to wild type in competition experiments performed in rich media. In culture conditions leading to slow growth, however, cells containing the wild-type sequence were the ultimate winner of the competition, emphasizing that the wild-type sequence is, in fact, the most fit solution for the S8-binding site.},
note = {0027-8424http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10639126
Journal Article},
keywords = {16S/genetics/metabolism Recombinant Fusion Proteins/genetics/metabolism Ribosomal Proteins/genetics/*metabolism Ribosomes/genetics/*metabolism Spectinomycin/pharmacology Support, Base Sequence Binding Sites/genetics Binding, Competitive Cell Division/genetics Cloning, Microbial Escherichia coli/drug effects/*genetics/metabolism Evolution, Molecular Drug Resistance, Molecular Protein Binding RNA, P.H.S. Variation (Genetics), Ribosomal, Ribosomal/genetics/*metabolism RNA, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}