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}
}
Barends S, Rudinger-Thirion J, Florentz C, Giege R, Pleij C W, Kraal B
tRNA-like structure regulates translation of Brome mosaic virus RNA Journal Article
In: J Virol, vol. 78, no. 8, pp. 4003-4010, 2004, ISBN: 15047816, (0022-538x Journal Article).
Abstract | Links | BibTeX | Tags: ase Sequence Bromovirus/*genetics/metabolism Genetic Complementation Test Genome, FLORENTZ, FRUGIER, Genetic Triticum/virology Tyrosine/chemistry Tyrosine-tRNA Ligase/chemistry/genetics/metabolism Viral Proteins/chemistry/genetics, Non-U.S. Gov't Translation, Transfer/chemistry/genetics RNA, Unité ARN, Viral Molecular Sequence Data Nucleic Acid Conformation RNA, Viral/*chemistry/*genetics Support
@article{,
title = {tRNA-like structure regulates translation of Brome mosaic virus RNA},
author = {S Barends and J Rudinger-Thirion and C Florentz and R Giege and C W Pleij and B Kraal},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15047816},
isbn = {15047816},
year = {2004},
date = {2004-01-01},
journal = {J Virol},
volume = {78},
number = {8},
pages = {4003-4010},
abstract = {For various groups of plant viruses, the genomic RNAs end with a tRNA-like structure (TLS) instead of the 3' poly(A) tail of common mRNAs. The actual function of these TLSs has long been enigmatic. Recently, however, it became clear that for turnip yellow mosaic virus, a tymovirus, the valylated TLS(TYMV) of the single genomic RNA functions as a bait for host ribosomes and directs them to the internal initiation site of translation (with N-terminal valine) of the second open reading frame for the polyprotein. This discovery prompted us to investigate whether the much larger TLSs of a different genus of viruses have a comparable function in translation. Brome mosaic virus (BMV), a bromovirus, has a tripartite RNA genome with a subgenomic RNA4 for coat protein expression. All four RNAs carry a highly conserved and bulky 3' TLS(BMV) (about 200 nucleotides) with determinants for tyrosylation. We discovered TLS(BMV)-catalyzed self-tyrosylation of the tyrosyl-tRNA synthetase but could not clearly detect tyrosine incorporation into any virus-encoded protein. We established that BMV proteins do not need TLS(BMV) tyrosylation for their initiation. However, disruption of the TLSs strongly reduced the translation of genomic RNA1, RNA2, and less strongly, RNA3, whereas coat protein expression from RNA4 remained unaffected. This aberrant translation could be partially restored by providing the TLS(BMV) in trans. Intriguingly, a subdomain of the TLS(BMV) could even almost fully restore translation to the original pattern. We discuss here a model with a central and dominant role for the TLS(BMV) during the BMV infection cycle.},
note = {0022-538x
Journal Article},
keywords = {ase Sequence Bromovirus/*genetics/metabolism Genetic Complementation Test Genome, FLORENTZ, FRUGIER, Genetic Triticum/virology Tyrosine/chemistry Tyrosine-tRNA Ligase/chemistry/genetics/metabolism Viral Proteins/chemistry/genetics, Non-U.S. Gov't Translation, Transfer/chemistry/genetics RNA, Unité ARN, Viral Molecular Sequence Data Nucleic Acid Conformation RNA, Viral/*chemistry/*genetics Support},
pubstate = {published},
tppubtype = {article}
}
Tryoen-Toth P, Richert S, Sohm B, Mine M, Marsac C, Dorsselaer A Van, Leize E, Florentz C
Proteomic consequences of a human mitochondrial tRNA mutation beyond the frame of mitochondrial translation Journal Article
In: J Biol Chem, vol. 278, no. 27, pp. 24314-24323, 2003, ISBN: 12714596, (0021-9258 Journal Article).
Abstract | Links | BibTeX | Tags: Cultured, FLORENTZ, Genetic Tumor Cells, Human Mitochondria/genetics *Mutation Nuclear Proteins/*genetics Proteomics RNA/*genetics RNA, Non-U.S. Gov't Translation, Transfer/*genetics Structure-Activity Relationship Support, Unité ARN
@article{,
title = {Proteomic consequences of a human mitochondrial tRNA mutation beyond the frame of mitochondrial translation},
author = {P Tryoen-Toth and S Richert and B Sohm and M Mine and C Marsac and A Van Dorsselaer and E Leize and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12714596},
isbn = {12714596},
year = {2003},
date = {2003-01-01},
journal = {J Biol Chem},
volume = {278},
number = {27},
pages = {24314-24323},
abstract = {Numerous severe neurodegenerative and neuromuscular disorders, characterized biochemically by strong perturbations in energy metabolism, are correlated with single point mutations in mitochondrial genes coding for transfer RNAs. Initial comparative proteomics performed on wild-type and Myoclonic Epilepsy and Ragged Red Fibers (MERRF) mitochondria from sibling human cybrid cell lines revealed the potential of this approach. Here a quantitative analysis of several hundred silver-stained spots separated by two-dimensional gel electrophoresis was performed in the specific case of a couple of mitochondria, containing or not mutation A8344G in the gene for mitochondrial tRNALys, correlated with MERRF syndrome. Computer-assisted analysis allowed us to detect 38 spots with significant quantitative variations, of which 20 could be assigned by mass spectrometry. These include nuclear encoded proteins located in mitochondria such as respiratory chain subunits, metabolic enzymes, a protein of the mitochondrial translation machinery, and cytosolic contaminants. Furthermore, Western blotting combined with mass spectrometry revealed the occurrence of numerous isoforms of pyruvate dehydrogenase subunits, with subtle changes in post-translational modifications. This comparative proteomic approach gives the first insight for nuclear encoded proteins that undergo the largest quantitative changes, and pinpoints new potential molecular partners involved in the cascade of events that connect genotype to phenotype.},
note = {0021-9258
Journal Article},
keywords = {Cultured, FLORENTZ, Genetic Tumor Cells, Human Mitochondria/genetics *Mutation Nuclear Proteins/*genetics Proteomics RNA/*genetics RNA, Non-U.S. Gov't Translation, Transfer/*genetics Structure-Activity Relationship Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Florentz C, Sohm B, Tryoen-Toth P, Putz J, Sissler M
Human mitochondrial tRNAs in health and disease Journal Article
In: Cell Mol Life Sci, vol. 60, no. 7, pp. 1356-1375, 2003, ISBN: 12943225, (1420-682x Journal Article Review Review, Academic).
Abstract | Links | BibTeX | Tags: Base Sequence Genetic Diseases, FLORENTZ, Genetic, Inborn/*genetics Genome Human Mitochondria/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/*genetics RNA, Messenger/genetics/metabolism RNA, Non-U.S. Gov't Translation, SISSLER, Transfer/chemistry/*genetics Reference Values Support, Unité ARN
@article{,
title = {Human mitochondrial tRNAs in health and disease},
author = {C Florentz and B Sohm and P Tryoen-Toth and J Putz and M Sissler},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12943225},
isbn = {12943225},
year = {2003},
date = {2003-01-01},
journal = {Cell Mol Life Sci},
volume = {60},
number = {7},
pages = {1356-1375},
abstract = {The human mitochondrial genome encodes 13 proteins, all subunits of the respiratory chain complexes and thus involved in energy metabolism. These genes are translated by 22 transfer RNAs (tRNAs), also encoded by the mitochondrial genome, which form the minimal set required for reading all codons. Human mitochondrial tRNAs gained interest with the rapid discovery of correlations between point mutations in their genes and various neuromuscular and neurodegenerative disorders. In this review, emerging fundamental knowledge on the structure/function relationships of these particular tRNAs and an overview of the large variety of mechanisms within translation, affected by mutations, are summarized. Also, initial results on wide-ranging molecular consequences of mutations outside the frame of mitochondrial translation are highlighted. While knowledge of mitochondrial tRNAs in both health and disease increases, deciphering the intricate network of events leading different genotypes to the variety of phenotypes requires further investigation using adapted model systems.},
note = {1420-682x
Journal Article
Review
Review, Academic},
keywords = {Base Sequence Genetic Diseases, FLORENTZ, Genetic, Inborn/*genetics Genome Human Mitochondria/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA/chemistry/*genetics RNA, Messenger/genetics/metabolism RNA, Non-U.S. Gov't Translation, SISSLER, Transfer/chemistry/*genetics Reference Values Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Fagegaltier D, Hubert N, Yamada K, Mizutani T, Carbon P, Krol A
Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation Journal Article
In: EMBO J, vol. 19, no. 17, pp. 4796-4805, 2000, ISBN: 10970870, (0261-4189 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Animals Bacterial Proteins/chemistry/*metabolism/physiology Caenorhabditis elegans/genetics Drosophila/genetics Hela Cells Human Mice Molecular Sequence Data Peptide Elongation Factors/chemistry/*metabolism/physiology Protein Binding Proteins/*genetics RNA, Amino Acyl/metabolism Sequence Homology, Genetic/*physiology, Non-U.S. Gov't Translation, Transfer, Unité ARN
@article{,
title = {Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation},
author = {D Fagegaltier and N Hubert and K Yamada and T Mizutani and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10970870},
isbn = {10970870},
year = {2000},
date = {2000-01-01},
journal = {EMBO J},
volume = {19},
number = {17},
pages = {4796-4805},
abstract = {Decoding of UGA selenocysteine codons in eubacteria is mediated by the specialized elongation factor SelB, which conveys the charged tRNA(Sec) to the A site of the ribosome, through binding to the SECIS mRNA hairpin. In an attempt to isolate the eukaryotic homolog of SelB, a database search in this work identified a mouse expressed sequence tag containing the complete cDNA encoding a novel protein of 583 amino acids, which we called mSelB. Several lines of evidence enabled us to establish that mSelB is the bona fide mammalian elongation factor for selenoprotein translation: it binds GTP, recognizes the Sec-tRNA(Sec) in vitro and in vivo, and is required for efficient selenoprotein translation in vivo. In contrast to the eubacterial SelB, the recombinant mSelB alone is unable to bind specifically the eukaryotic SECIS RNA hairpin. However, complementation with HeLa cell extracts led to the formation of a SECIS-dependent complex containing mSelB and at least another factor. Therefore, the role carried out by a single elongation factor in eubacterial selenoprotein translation is devoted to two or more specialized proteins in eukaryotes.},
note = {0261-4189
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Animals Bacterial Proteins/chemistry/*metabolism/physiology Caenorhabditis elegans/genetics Drosophila/genetics Hela Cells Human Mice Molecular Sequence Data Peptide Elongation Factors/chemistry/*metabolism/physiology Protein Binding Proteins/*genetics RNA, Amino Acyl/metabolism Sequence Homology, Genetic/*physiology, Non-U.S. Gov't Translation, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Hubert N, Walczak R, Carbon P, Krol A
A protein binds the selenocysteine insertion element in the 3'-UTR of mammalian selenoprotein mRNAs Journal Article
In: Nucleic Acids Res, vol. 24, no. 3, pp. 464-469, 1996, ISBN: 8602359, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence DNA Transposable Elements/*genetics Molecular Sequence Data Protein Binding Proteins/*genetics/metabolism RNA, Genetic, Messenger/genetics/*metabolism Rats Selenocysteine/genetics/*metabolism Support, Non-U.S. Gov't Translation, Unité ARN
@article{,
title = {A protein binds the selenocysteine insertion element in the 3'-UTR of mammalian selenoprotein mRNAs},
author = {N Hubert and R Walczak and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8602359},
isbn = {8602359},
year = {1996},
date = {1996-01-01},
journal = {Nucleic Acids Res},
volume = {24},
number = {3},
pages = {464-469},
abstract = {Several gene products are involved in co-translational insertion of selenocysteine by the tRNA(Sec). In addition, a stem-loop structure in the mRNAs coding for selenoproteins is essential to mediate the selection of the proper selenocysteine UGA codon. Interestingly, in eukaryotic selenoprotein mRNAs, this stem-loop structure, the selenocysteine insertion sequence (SECIS) element, resides in the 3'-untranslated region, far downstream of the UGA codon. In view of unravelling the underlying complex mechanism, we have attempted to detect RNA-binding proteins with specificity for the SECIS element. Using mobility shift assays, we could show that a protein, present in different types of mammalian cell extracts, possesses the capacity of binding the SECIS element of the selenoprotein glutathione peroxidase (GPx) mRNA. We have termed this protein SBP, for Secis Binding Protein. Competition experiments attested that the binding is highly specific and UV cross-linking indicated that the protein has an apparent molecular weight in the range of 60-65 kDa. Finally, some data suggest that the SECIS elements in the mRNAs of GPx and another selenoprotein, type I iodothyronine 5' deiodinase, recognize the same SBP protein. This constitutes the first report of the existence of a 3' UTR binding protein possibly involved in the eukaryotic selenocysteine insertion mechanism.},
note = {0305-1048
Journal Article},
keywords = {Animals Base Sequence DNA Transposable Elements/*genetics Molecular Sequence Data Protein Binding Proteins/*genetics/metabolism RNA, Genetic, Messenger/genetics/*metabolism Rats Selenocysteine/genetics/*metabolism Support, Non-U.S. Gov't Translation, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Blomberg P, Engdahl H M, Malmgren C, Romby P, Wagner E G
In: Mol Microbiol, vol. 12, no. 1, pp. 49-60, 1994, ISBN: 7520116, (0950-382x Journal Article).
Abstract | Links | BibTeX | Tags: Antisense/chemistry/*physiology RNA, Bacterial Models, Bacterial Proteins/genetics/*metabolism Base Sequence Binding Sites *DNA Replication *Gene Expression Regulation, Bacterial/*genetics Reading Frames Ribosomes/*metabolism Sequence Alignment Support, Genetic, Genetic Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Peptides/*genetics/physiology *Proteins R Factors/*genetics RNA, Non-U.S. Gov't Translation, ROMBY, Unité ARN
@article{,
title = {Replication control of plasmid R1: disruption of an inhibitory RNA structure that sequesters the repA ribosome-binding site permits tap-independent RepA synthesis},
author = {P Blomberg and H M Engdahl and C Malmgren and P Romby and E G Wagner},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7520116},
isbn = {7520116},
year = {1994},
date = {1994-01-01},
journal = {Mol Microbiol},
volume = {12},
number = {1},
pages = {49-60},
abstract = {The replication frequency of plasmid R1 is controlled by an antisense RNA, CopA, that inhibits the synthesis of the replication initiator protein, RepA, at the post-transcriptional level. This inhibition is indirect and affects translation of a leader peptide reading frame (tap). Translation of tap is required for repA translation (Blomberg et al., 1992). Here we asked whether an RNA stem-loop sequestering the repA ribosome-binding site blocks tap translation-independent repA expression. Destabilization of this structure resulted in tap-independent RepA synthesis, concomitant with a loss of CopA-mediated inhibition; thus, CopA acts at the level of tap translation. Structure probing of RepA mRNAs confirmed that the introduced mutations induced a local destabilization in the repA ribosome-binding site stem-loop. An increased spacing between the repA Shine-Dalgarno region and the start codon permitted even higher repA expression. In Incl alpha/IncB plasmids, an RNA pseudoknot acts as an activator for rep translation. We suggest that the regulatory pathway in plasmid R1 does not involve an activator RNA pseudoknot.},
note = {0950-382x
Journal Article},
keywords = {Antisense/chemistry/*physiology RNA, Bacterial Models, Bacterial Proteins/genetics/*metabolism Base Sequence Binding Sites *DNA Replication *Gene Expression Regulation, Bacterial/*genetics Reading Frames Ribosomes/*metabolism Sequence Alignment Support, Genetic, Genetic Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Peptides/*genetics/physiology *Proteins R Factors/*genetics RNA, Non-U.S. Gov't Translation, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Skripkin E, Yusupova G, Yusupov M, Kessler P, Ehresmann C, Ehresmann B
Synthesis and ribosome binding properties of model mRNAs modified with undecagold cluster Journal Article
In: Bioconjug Chem, vol. 4, no. 6, pp. 549-553, 1993, ISBN: 8305524, (1043-1802 Journal Article).
Abstract | Links | BibTeX | Tags: Base Sequence Comparative Study Escherichia coli/metabolism Gold/metabolism Models, Genetic/drug effects/genetics, Messenger/*chemical synthesis/chemistry/*metabolism RNA, Met/metabolism Ribosomes/*metabolism Support, Molecular Molecular Sequence Data Organometallic Compounds/*chemical synthesis/chemistry/*metabolism RNA, Non-U.S. Gov't Translation, Transfer, Unité ARN
@article{,
title = {Synthesis and ribosome binding properties of model mRNAs modified with undecagold cluster},
author = {E Skripkin and G Yusupova and M Yusupov and P Kessler and C Ehresmann and B Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8305524},
isbn = {8305524},
year = {1993},
date = {1993-01-01},
journal = {Bioconjug Chem},
volume = {4},
number = {6},
pages = {549-553},
abstract = {The synthesis and purification of short model messenger RNAs modified with undecagold cluster are described. A monoamino undecagold cluster was introduced on the oxidized 3' cis-glycol group of the mRNA followed by reduction of the formed Schiff's base. The stability of the modified mRNA under the conditions used for in vitro messenger RNA translation is studied. The possibility of the formation of a specific translational initiation complex with bacterial ribosomes and modified mRNAs is shown. The results of these experiments indicate that the attachment of an undecagold cluster to a mRNA is a useful tool for electron microscopic and crystallographic studies.},
note = {1043-1802
Journal Article},
keywords = {Base Sequence Comparative Study Escherichia coli/metabolism Gold/metabolism Models, Genetic/drug effects/genetics, Messenger/*chemical synthesis/chemistry/*metabolism RNA, Met/metabolism Ribosomes/*metabolism Support, Molecular Molecular Sequence Data Organometallic Compounds/*chemical synthesis/chemistry/*metabolism RNA, Non-U.S. Gov't Translation, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Baudin F, Marquet R, Isel C, Darlix J L, Ehresmann B, Ehresmann C
Functional sites in the 5' region of human immunodeficiency virus type 1 RNA form defined structural domains Journal Article
In: J Mol Biol, vol. 229, no. 2, pp. 382-397, 1993, ISBN: 8429553, (0022-2836 Journal Article).
Abstract | Links | BibTeX | Tags: Animals Base Sequence Electrophoresis, Genetic, MARQUET, Non-U.S. Gov't Translation, Polyacrylamide Gel HIV-1/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Unité ARN, Viral/*chemistry/metabolism Rabbits Support
@article{,
title = {Functional sites in the 5' region of human immunodeficiency virus type 1 RNA form defined structural domains},
author = {F Baudin and R Marquet and C Isel and J L Darlix and B Ehresmann and C Ehresmann},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8429553},
isbn = {8429553},
year = {1993},
date = {1993-01-01},
journal = {J Mol Biol},
volume = {229},
number = {2},
pages = {382-397},
abstract = {The 5' region of HIV-1 RNA contains functional elements involved in key steps of the retroviral cycle, such as genomic RNA transcription, splicing, translation, dimerization or initiation of reverse transcription. In the present work, we investigated the conformation of the first 500 nucleotides covering the RNA leader and the 5' gag coding sequences of HIV-MAL, using chemical probing. We provide detailed information on almost each nucleotide at one of their Watson-Crick positions and on position N-7 of purines. Experiments were conducted on two in vitro transcribed RNA fragments (1 to 707 and 1 to 311). A secondary structure model was derived by combining the experimental data, computer predictions and sequence comparison. Under conditions favoring dimerization (high salt concentration), HIV-1 RNA folds into independent structural domains that can be related to defined functional regions. The first domain corresponds to TAR forming a stable stem-loop. Intrinsic structural features are found to stabilize the TAR hairpin loop. The second domain (nucleotides 56 to 299) contains the PBS sequence, which is located in a stable subdomain constrained by a four stem junction (nucleotides 139 to 218). Although the MAL isolate has an insertion near the PBS, probably resulting from the duplication of a 23-nucleotide sequence, the structural organization of this subdomain is conserved in all other HIV-1 isolates. The third domain (nucleotides 300 to 404) contains the splice donor site, packaging and dimerization elements and the AUG initiation codon of gag. A major result is the structural versatility of this region. Two mutually exclusive structures, both equally in agreement with probing data, could modulate the different functions involving this domain. The reduced accessibility of the gag translational initiation site possibly accounts for the low efficiency of the in vitro translation of the dimer. Finally, the 5' gag coding sequences form a metastable domain.},
note = {0022-2836
Journal Article},
keywords = {Animals Base Sequence Electrophoresis, Genetic, MARQUET, Non-U.S. Gov't Translation, Polyacrylamide Gel HIV-1/*genetics Molecular Sequence Data Nucleic Acid Conformation RNA, Unité ARN, Viral/*chemistry/metabolism Rabbits Support},
pubstate = {published},
tppubtype = {article}
}