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Brulé-Morabito Fabienne


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tél : 02.38.25.55.86 - fax : 02.38.25.55.83

Publications

2013   Références trouvées : 1

Mollet L., Robinet P., Dubois M., Aurouet A., Normand T., Charpentier S., Sureau A., Grandclement C., Garnache-Ottou F., Deconinck E., Brulé F., Rohrlich P.S. and Legrand A.  (2013)

Opposing Mcl-1, the GALIG proapoptotic gene is upregulated as neutrophils die and underexpressed in Acute Myeloid Leukemia cells

Molecular Immunology 56 (1-2) 123-128
GALIG gene expression induces apoptosis in cultured cells through a pathway still under investigation. It is highly expressed in leukocytes but weakly detectable in bone marrow, suggesting a role in the myeloid lineage homeostasis. We show here that GALIG-induced cell death is counteracted by the overexpression of MCL-1, a pro-survival member of the Bcl2 family. Moreover, during spontaneous neutrophil apoptosis, a substantial increase in GALIG gene expression is observed : GALIG still opposes MCL-1. Finally, in bone marrow and peripheral blood cells from patients with Acute Myeloid Leukemia type 2, the level of GALIG transcripts is massively down-regulated when compared to their normal counterparts, while MCL-1 is expressed to the same extent. These data suggest that GALIG could be a key player in the cell death pathway involved in leukocytes homeostasis and myeloid malignancies.

GALIG gene expression induces apoptosis in cultured cells through a pathway still under investigation. It is highly expressed in leukocytes but weakly detectable in bone marrow, suggesting a role in the myeloid lineage homeostasis. We show here that GALIG-induced cell death is counteracted by the overexpression of MCL-1, a pro-survival member of the Bcl2 family. Moreover, during spontaneous neutrophil apoptosis, a substantial increase in GALIG gene expression is observed : GALIG still opposes MCL-1. Finally, in bone marrow and peripheral blood cells from patients with Acute Myeloid Leukemia type 2, the level of GALIG transcripts is massively down-regulated when compared to their normal counterparts, while MCL-1 is expressed to the same extent. These data suggest that GALIG could be a key player in the cell death pathway involved in leukocytes homeostasis and myeloid malignancies.


2010   Références trouvées : 1

Robinet, P., Mollet, L., Gonzalez, P., Normand, T., Charpentier, S., Brule, F., Dubois, M. & Legrand, A.  (2010)

The mitogaligin protein is addressed to the nucleus via a non-classical localization signal.

Biochem. Biophys. Res. Commun. 392, 53-57.


2008   Références trouvées : 1

Benoit R., Saboungi M.-L. et Brulé F.  (2008)

Nouveau matériau à propriétés bactériostatiques

Brevet déposé à l’INPI, N° de dépôt FR08 00570, déposants CNRS, Université d’Orléans.


2006   Références trouvées : 1

Kieken, F ; Paquet, F ; Brule, F ; Paoletti, J ; Lancelot, G  (2006)

A new NMR solution structure of the SL1 HIV-1(Lai) loop-loop dimer

Nucleic Acids Research 34 (1) 343-352
Dimerization of genomic RNA is directly related with the event of encapsidation and maturation of the virion. The initiating sequence of the dimerization is a short autocomplementary region in the hairpin loop SL1. We describe here a new solution structure of the RNA dimerization initiation site (DIS) of HIV-1(Lai). NMR pulsed field-gradient spin-echo techniques and multidimensional heteronuclear NMR spectroscopy indicate that this structure is formed by two hairpins linked by six Watson-Crick GC base pairs. Hinges between the stems and the loops are stabilized by intra and intermolecular interactions involving the A8, A9 and A16 adenines. The coaxial alignment of the three A-type helices present in the structure is supported by previous crystallography analysis but the A8 and A9 adenines are found in a bulged in position. These data suggest the existence of an equilibrium between bulged in and bulged out conformations in solution.

Dimerization of genomic RNA is directly related with the event of encapsidation and maturation of the virion. The initiating sequence of the dimerization is a short autocomplementary region in the hairpin loop SL1. We describe here a new solution structure of the RNA dimerization initiation site (DIS) of HIV-1(Lai). NMR pulsed field-gradient spin-echo techniques and multidimensional heteronuclear NMR spectroscopy indicate that this structure is formed by two hairpins linked by six Watson-Crick GC base pairs. Hinges between the stems and the loops are stabilized by intra and intermolecular interactions involving the A8, A9 and A16 adenines. The coaxial alignment of the three A-type helices present in the structure is supported by previous crystallography analysis but the A8 and A9 adenines are found in a bulged in position. These data suggest the existence of an equilibrium between bulged in and bulged out conformations in solution.


2003   Références trouvées : 1

Rigourd, M ; Goldschmidt, V ; Brule, F ; Morrow, CD ; Ehresmann, B ; Ehresmann, C ; Marquet, R  (2003)

Structure-function relationships of the initiation complex of HIV-1 reverse transcription : the case of mutant viruses using tRNA(His) as primer

Nucleic Acids Research 31 (19) 5764-5775
Reverse transcription of HIV-1 RNA is initiated from the 3' end of a tRNA(3)(Lys) molecule annealed to the primer binding site (PBS). An additional interaction between the anticodon loop of tRNA(3)(Lys) and a viral A-rich loop is required for efficient initiation of reverse transcription of the HIV-1 MAL isolate. In the HIV-1 HXB2 isolate, simultaneous mutations of the PBS and the A-rich loop (mutant His-AC), but not of the PBS alone (mutant His) allows the virus to stably utilize tRNA(His) as primer. However, mutant His-AC selects additional mutations during cell culture, generating successively His-AC-GAC and His-AC-AT-GAC. Here, we wanted to establish direct relationships between the evolution of these mutants in cell culture, their efficiency in initiating reverse transcription and the structure of the primer/template complexes in vitro.

Reverse transcription of HIV-1 RNA is initiated from the 3’ end of a tRNA(3)(Lys) molecule annealed to the primer binding site (PBS). An additional interaction between the anticodon loop of tRNA(3)(Lys) and a viral A-rich loop is required for efficient initiation of reverse transcription of the HIV-1 MAL isolate. In the HIV-1 HXB2 isolate, simultaneous mutations of the PBS and the A-rich loop (mutant His-AC), but not of the PBS alone (mutant His) allows the virus to stably utilize tRNA(His) as primer. However, mutant His-AC selects additional mutations during cell culture, generating successively His-AC-GAC and His-AC-AT-GAC. Here, we wanted to establish direct relationships between the evolution of these mutants in cell culture, their efficiency in initiating reverse transcription and the structure of the primer/template complexes in vitro.


2002   Références trouvées : 1

Brule, F ; Marquet, R ; Rong, L ; Wainberg, MA ; Roques, BP ; Le Grice, SFJ ; Ehresmann, B ; Ehresmann, C  (2002)

Structural and functional properties of the HIV-1 RNA-tRN(3)(Lys) primer complex annealed by the nucleocapsid protein : Comparison with the heat-annealed complex

Rna-A Publication of The Rna Society 8 (1) 8-15
The conversion of the single-stranded RNA genome into double-stranded DNA by virus-coded reverse transcriptase (RT) is an essential step of the retrovirus life cycle. In human immunodeficiency virus type 1 (HIV-1), RT uses the cellular tRNA(3)(Lys) to initiate the (-) strand DNA synthesis. Placement of the primer tRNA(3)(Lys) involves binding of its 3'-terminal 18 nt to a complementary region of genomic RNA termed PBS. However, the PBS sequence is not the unique determinant of primer usage and additional contacts are important. This placement is believed to be achieved in vivo by the nucleocapsid domain of Gag or by the mature protein NCp. Up to now, structural information essentially arose from heat-annealed primer-template complexes (Isel et al., J Mol Biol, 1995, 247:236-250 ; Isel et al., EMBO J, 1999, 18:1038-1048).

The conversion of the single-stranded RNA genome into double-stranded DNA by virus-coded reverse transcriptase (RT) is an essential step of the retrovirus life cycle. In human immunodeficiency virus type 1 (HIV-1), RT uses the cellular tRNA(3)(Lys) to initiate the (-) strand DNA synthesis. Placement of the primer tRNA(3)(Lys) involves binding of its 3’-terminal 18 nt to a complementary region of genomic RNA termed PBS. However, the PBS sequence is not the unique determinant of primer usage and additional contacts are important. This placement is believed to be achieved in vivo by the nucleocapsid domain of Gag or by the mature protein NCp. Up to now, structural information essentially arose from heat-annealed primer-template complexes (Isel et al., J Mol Biol, 1995, 247:236-250 ; Isel et al., EMBO J, 1999, 18:1038-1048).


2000   Références trouvées : 1

Brule, F ; Bec, G ; Keith, G ; Le Grice, SFJ ; Roques, BP ; Ehresmann, B ; Ehresmann, C ; Marquet, R  (2000)

In vitro evidence for the interaction of tRNA(3)(Lys) With U3 during the first strand transfer of HIV-1 reverse transcription

Nucleic Acids Research 28 (2) 634-640
Over the course of its evolution, HIV-1 has taken maximum advantage of its tRNA(3)(Lys) primer by utilizing it in several steps of reverse transcription. Here, we have identified a conserved nonanucleotide sequence in the U3 region of HIV-1 RNA that is complementary to the anticodon stem of tRNA(3)(Lys). In order to test its possible role in the first strand transfer reaction, we applied an assay using a donor RNA corresponding to the 5'-part and an acceptor RNA spanning the 3'-part of HIV-1 RNA. In addition, we constructed two acceptor RNAs in which the nonanucleotide sequence complementary to tRNA(3)(Lys) was either substituted (S) or deleted (Delta).

Over the course of its evolution, HIV-1 has taken maximum advantage of its tRNA(3)(Lys) primer by utilizing it in several steps of reverse transcription. Here, we have identified a conserved nonanucleotide sequence in the U3 region of HIV-1 RNA that is complementary to the anticodon stem of tRNA(3)(Lys). In order to test its possible role in the first strand transfer reaction, we applied an assay using a donor RNA corresponding to the 5’-part and an acceptor RNA spanning the 3’-part of HIV-1 RNA. In addition, we constructed two acceptor RNAs in which the nonanucleotide sequence complementary to tRNA(3)(Lys) was either substituted (S) or deleted (Delta).


1998   Références trouvées : 1

Fournier, R ; Brule, F ; Segault, V ; Mougin, A ; Branlant, C  (1998)

U3 snoRNA genes with and without intron in the Kluyveromyces genus : Yeasts can accommodate great variations of the U3 snoRNA 3 ’-terminal domain

Rna-A Publication of The Rna Society 4 (3) 285-302
The U3 snoRNA coding sequences from the genomic DNAs of Kluyveromyces delphensis and four variants of the Kluyveromyces marxianus species were cloned by PCR amplification. Nucleotide sequence analysis of the amplification products revealed a unique U3 snoRNA gene sequence in all the strains studied, except for K. marxianus var. fragilis. The K. marxianus U3 genes were intronless, whereas an intron similar to those of the Saccharomyces cerevisiae U3 genes was found in K. delphensis. Hence, U3 genes with and without intron are found in yeasts of the Saccharomycetoideae subfamily. The secondary structure of the K. delphensis pre-U3 snoRNA and of the K. marxianus mature snoRNAs were studied experimentally.

The U3 snoRNA coding sequences from the genomic DNAs of Kluyveromyces delphensis and four variants of the Kluyveromyces marxianus species were cloned by PCR amplification. Nucleotide sequence analysis of the amplification products revealed a unique U3 snoRNA gene sequence in all the strains studied, except for K. marxianus var. fragilis. The K. marxianus U3 genes were intronless, whereas an intron similar to those of the Saccharomyces cerevisiae U3 genes was found in K. delphensis. Hence, U3 genes with and without intron are found in yeasts of the Saccharomycetoideae subfamily. The secondary structure of the K. delphensis pre-U3 snoRNA and of the K. marxianus mature snoRNAs were studied experimentally.


1997   Références trouvées : 1

Herbin, S ; Mathieu, F ; Brule, F ; Branlant, C ; Lefebvre, G ; Lebrihi, A  (1997)

Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese

Current Microbiology 35 (6) 319-326
Carnobacterium piscicola CP5, isolated from a French mold-ripened soft cheese, produced a bacteriocin activity named carnocin CP5, which inhibited Carnobacterium, Enterococcus and Listeria spp. strains, and among the Lactobacillus spp. only Lactobacillus delbrueckii spp. [24]. The activity was purified by ammonium sulfate precipitation, anion exchange, and hydrophobic interaction chromatography followed by reverse-phase high-performance liquid chromatography (RP-HPLC). This latter step separated two peaks with anti-listerial activity (CP51 and CP52). Carnocin CP51 was partially sequenced, and the N-terminal part revealed the presence of the ''pediocin-like consensus'' sequence-Tyr-Gly-Asn-Gly-Val-. Then, a degenerated 24-mer oligonucleotide probe was constructed from the N-terminal sequence and used to detect the structural gene. It was localized on a plasmid of about 40 kb.

Carnobacterium piscicola CP5, isolated from a French mold-ripened soft cheese, produced a bacteriocin activity named carnocin CP5, which inhibited Carnobacterium, Enterococcus and Listeria spp. strains, and among the Lactobacillus spp. only Lactobacillus delbrueckii spp. [24]. The activity was purified by ammonium sulfate precipitation, anion exchange, and hydrophobic interaction chromatography followed by reverse-phase high-performance liquid chromatography (RP-HPLC). This latter step separated two peaks with anti-listerial activity (CP51 and CP52). Carnocin CP51 was partially sequenced, and the N-terminal part revealed the presence of the ’’pediocin-like consensus’’ sequence-Tyr-Gly-Asn-Gly-Val-. Then, a degenerated 24-mer oligonucleotide probe was constructed from the N-terminal sequence and used to detect the structural gene. It was localized on a plasmid of about 40 kb.


1996   Références trouvées : 2

Brule, F ; Venema, J ; Segault, V ; Tollervey, D ; Branlant, C  (1996)

The yeast Hansenula wingei U3 snoRNA gene contains an intron and its coding sequence co-evolved with the 5’ ETS region of the pre-ribosomal RNA

Rna-A Publication of The Rna Society 2 (2) 183-197
The 5' external transcribed spacer (ETS) region of the pre-rRNA in Saccharomyces cerevisiae contains a sequence with 10 bp of perfect complementarity to the U3 snoRNA. Base pairing between these sequences has been shown to be required for 18S rRNA synthesis, although interaction over the full in bp of complementarity is not required. We have identified the homologous sequence in the 5' ETS from the evolutionarily distant yeast Hansenula wingei ; unexpectedly, this shows two sequence changes in the region predicted to base pair to U3. By PCR amplification and direct RNA sequencing, a single type of U3 snoRNA coding sequence was identified in H. wingei. As in the S. cerevisiae U3 snoRNA genes, it is interrupted by an intron with features characteristic of introns spliced in a spliceosome. Consequently, this unusual property is not restricted to the yeast genus Saccharomyces.

The 5’ external transcribed spacer (ETS) region of the pre-rRNA in Saccharomyces cerevisiae contains a sequence with 10 bp of perfect complementarity to the U3 snoRNA. Base pairing between these sequences has been shown to be required for 18S rRNA synthesis, although interaction over the full in bp of complementarity is not required. We have identified the homologous sequence in the 5’ ETS from the evolutionarily distant yeast Hansenula wingei ; unexpectedly, this shows two sequence changes in the region predicted to base pair to U3. By PCR amplification and direct RNA sequencing, a single type of U3 snoRNA coding sequence was identified in H. wingei. As in the S. cerevisiae U3 snoRNA genes, it is interrupted by an intron with features characteristic of introns spliced in a spliceosome. Consequently, this unusual property is not restricted to the yeast genus Saccharomyces.

Mougin, A ; Gregoire, A ; Banroques, J ; Segault, V ; Fournier, R ; Brule, F ; ChevrierMiller, M ; Branlant, C  (1996)

Secondary structure of the yeast Saccharomyces cerevisiae pre-U3A snoRNA and its implication for splicing efficiency

Rna-A Publication of The Rna Society 2 (11) 1079-1093
The Saccharomyces cerevisiae U3 snoRNA genes contain long spliceosomal introns with noncanonical branch site sequences. By using chemical and enzymatic methods to probe the RNA secondary structure and site-directed mutagenesis, we established the complete secondary structure of the U3A snoRNA precursor. This is the first determination of the complete secondary structure of an RNA spliced in a spliceosome. The peculiar cruciform structure of the U3A snoRNA 3'-terminal region is formed in the precursor RNA and the conserved Boxes B and C are accessible for binding the U3 snoRNP proteins. The intron forms a highly folded structure with a long central stem-loop structure that brings the 5' box and the branch site together.

The Saccharomyces cerevisiae U3 snoRNA genes contain long spliceosomal introns with noncanonical branch site sequences. By using chemical and enzymatic methods to probe the RNA secondary structure and site-directed mutagenesis, we established the complete secondary structure of the U3A snoRNA precursor. This is the first determination of the complete secondary structure of an RNA spliced in a spliceosome. The peculiar cruciform structure of the U3A snoRNA 3’-terminal region is formed in the precursor RNA and the conserved Boxes B and C are accessible for binding the U3 snoRNP proteins. The intron forms a highly folded structure with a long central stem-loop structure that brings the 5’ box and the branch site together.


1995   Références trouvées : 1

Brule, F ; Gregoire, A ; Segault, V ; Mougin, A ; Branlant, C  (1995)

Secondary structure conservation of the U3 small nucleolar RNA introns in Saccharomyces

Comptes Rendus de L Academie Des Sciences Serie Iii-Sciences de la Vie-Life Sciences 318 (12) 1197-1206


Mots-clés

Maître de conférences , Mort cellulaire programmée