Publications
2009
Kachouri-Lafond R, Dujon B, Gilson E, Westhof E, Fairhead C, Teixeira M T
Large telomerase RNA, telomere length heterogeneity and escape from senescence in Candida glabrata Journal Article
In: FEBS Lett, vol. 583, no. 22, pp. 3605-3610, 2009, ISBN: 19840797, (1873-3468 (Electronic) 0014-5793 (Linking) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: Base Sequence Blotting, Fungal/chemistry/*genetics Sequence Homology, Fungal/genetics Flow Cytometry Gene Deletion Molecular Sequence Data Mutation Nucleic Acid Conformation RNA/chemistry/*genetics RNA, Nucleic Acid Telomerase/chemistry/*genetics Telomere/*genetics, Southern Candida glabrata/enzymology/*genetics/growth & development Cell Division DNA, Unité ARN, WESTHOF
@article{,
title = {Large telomerase RNA, telomere length heterogeneity and escape from senescence in Candida glabrata},
author = {R Kachouri-Lafond and B Dujon and E Gilson and E Westhof and C Fairhead and M T Teixeira},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19840797},
isbn = {19840797},
year = {2009},
date = {2009-01-01},
journal = {FEBS Lett},
volume = {583},
number = {22},
pages = {3605-3610},
abstract = {Telomerase, the key enzyme essential for the maintenance of eukaryotic chromosome ends, contains a reverse transcriptase and an RNA that provides the template for the synthesis of telomeric repeats. Here, we characterize the telomerase subunits in the hemiascomycete yeast Candida glabrata. We propose a secondary structure model for the telomerase RNA that is the largest described to date. Telomerase deletion mutants show a progressive shortening of telomeres and a modest loss of viability. Frequent post-senescence survivors emerge that possess long telomeric repeat tracts. We suggest that the high telomere length heterogeneity accounts for this distinct senescence phenotype.},
note = {1873-3468 (Electronic)
0014-5793 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {Base Sequence Blotting, Fungal/chemistry/*genetics Sequence Homology, Fungal/genetics Flow Cytometry Gene Deletion Molecular Sequence Data Mutation Nucleic Acid Conformation RNA/chemistry/*genetics RNA, Nucleic Acid Telomerase/chemistry/*genetics Telomere/*genetics, Southern Candida glabrata/enzymology/*genetics/growth & development Cell Division DNA, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}
2004
Malnou C E, Werner A, Borman A M, Westhof E, Kean K M
Effects of vaccine strain mutations in domain V of the internal ribosome entry segment compared in the wild type poliovirus type 1 context Journal Article
In: J Biol Chem, vol. 279, no. 11, pp. 10261-10269, 2004, ISBN: 14672927, (0021-9258 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence Blotting, Genetic, Messenger/metabolism Ribosomes/*genetics Support, Non-U.S. Gov't Translation, Tertiary RNA/chemistry RNA, Unité ARN, Viral Electrophoresis, Western DNA, WESTHOF
@article{,
title = {Effects of vaccine strain mutations in domain V of the internal ribosome entry segment compared in the wild type poliovirus type 1 context},
author = {C E Malnou and A Werner and A M Borman and E Westhof and K M Kean},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14672927},
isbn = {14672927},
year = {2004},
date = {2004-01-01},
journal = {J Biol Chem},
volume = {279},
number = {11},
pages = {10261-10269},
abstract = {Initiation of poliovirus (PV) protein synthesis is governed by an internal ribosome entry segment structured into several domains including domain V, which is accepted to be important in PV neurovirulence because it harbors an attenuating mutation in each of the vaccine strains developed by A. Sabin. To better understand how these single point mutations exert their effects, we placed each of them into the same genomic context, that of PV type 1. Only the mutation equivalent to the Sabin type 3 strain mutation resulted in significantly reduced viral growth both in HeLa and neuroblastoma cells. This correlated with poor translation efficiency in vitro and could be explained by a structural perturbation of the domain V of the internal ribosome entry segment, as evidenced by RNA melting experiments. We demonstrated that reduced cell death observed during infection by this mutant is due to the absence of inhibition of host cell translation. We confirmed that this shut-off is correlated principally with cleavage of eIF4GII and not eIF4GI and that this cleavage is significantly impaired in the case of the defective mutant. These data support the previously reported conclusion that the 2A protease has markedly different affinities for the two eIF4G isoforms.},
note = {0021-9258
Journal Article},
keywords = {Base Sequence Blotting, Genetic, Messenger/metabolism Ribosomes/*genetics Support, Non-U.S. Gov't Translation, Tertiary RNA/chemistry RNA, Unité ARN, Viral Electrophoresis, Western DNA, WESTHOF},
pubstate = {published},
tppubtype = {article}
}