Characterization of Unique Signature Sequences in the Divergent Maternal Protein Bcl2l10
| Autor: | Germain Gillet, Abdel Aouacheria, François Penin, Aurélie Cornut-Thibaut, Yannis Guillemin |
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| Přispěvatelé: | Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Ganivet, Agnès, Institut de biologie et chimie des protéines [Lyon] ( IBCP ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Centre de Recherche en Cancérologie de Lyon ( CRCL ), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie Moléculaire de la Cellule ( LBMC ), École normale supérieure - Lyon ( ENS Lyon ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL) |
| Rok vydání: | 2011 |
| Předmět: |
MESH : Cell Line
MESH : Molecular Sequence Data Amino Acid Motifs MESH: Amino Acid Sequence MESH: Base Sequence MESH : Proto-Oncogene Proteins c-bcl-2 [ SDV.CAN ] Life Sciences [q-bio]/Cancer MESH: INDEL Mutation protein sequence MESH: Amino Acid Motifs MESH: Protein Structure Tertiary 0302 clinical medicine INDEL Mutation Databases Genetic genetic polymorphism MESH : Female MESH: Animals MESH: Genetic Variation [SDV.BDD]Life Sciences [q-bio]/Development Biology Peptide sequence MESH: Databases Genetic MESH: Evolution Molecular Sequence Deletion Genetics chemistry.chemical_classification 0303 health sciences MESH : Amino Acid Sequence MESH : Sequence Alignment apoptosis Vertebrate MESH: Sequence Deletion Amino acid Proto-Oncogene Proteins c-bcl-2 MESH: Calcium 030220 oncology & carcinogenesis Female MESH : Protein Structure Tertiary MESH : Amino Acid Motifs Molecular Sequence Data MESH: Sequence Alignment [SDV.CAN]Life Sciences [q-bio]/Cancer Sequence alignment Biology Cell Line MESH: Oocytes Evolution Molecular 03 medical and health sciences Bcl-2 family MESH : Genetic Variation biology.animal evolution [SDV.BDD] Life Sciences [q-bio]/Development Biology Genetic variation Homologous chromosome Animals Humans MESH : HeLa Cells MESH : Evolution Molecular Amino Acid Sequence MESH : Calcium MESH : Databases Genetic Indel MESH : INDEL Mutation Molecular Biology Ecology Evolution Behavior and Systematics 030304 developmental biology MESH : Mutagenesis Insertional calcium MESH: Humans MESH: Molecular Sequence Data Base Sequence MESH : Sequence Deletion MESH: Apoptosis MESH : Humans MESH : Oocytes Genetic Variation Protein Structure Tertiary MESH: Cell Line Mutagenesis Insertional MESH: Mutagenesis Insertional MESH: Proto-Oncogene Proteins c-bcl-2 chemistry MESH: HeLa Cells Oocytes MESH : Base Sequence MESH : Animals Sequence Alignment MESH: Female MESH : Apoptosis HeLa Cells |
| Zdroj: | Molecular Biology and Evolution Molecular Biology and Evolution, Oxford University Press (OUP), 2011, 28 (12), pp.3271-83. ⟨10.1093/molbev/msr152⟩ Molecular Biology and Evolution, Oxford University Press (OUP), 2011, 28 (12), pp.3271-83. 〈10.1093/molbev/msr152〉 Molecular Biology and Evolution, Oxford University Press (OUP), 2011, 28 (12), pp.3271-3283 Molecular Biology and Evolution, 2011, 28 (12), pp.3271-83. ⟨10.1093/molbev/msr152⟩ Molecular Biology and Evolution, 2011, 28 (12), pp.3271-3283 |
| ISSN: | 1537-1719 0737-4038 |
| DOI: | 10.1093/molbev/msr152 |
| Popis: | International audience; Insertions or deletions (indels) of amino acids residues have been recognized as an important source of genetic and structural divergence between paralogous Bcl-2 family members. However, these signature sequences have not so far been extensively investigated amongst orthologous Bcl-2 family proteins. Bcl2l10 is an antiapoptotic member of the Bcl-2 family that has evolved rapidly throughout the vertebrate lineage and which shows conserved abundant expression in eggs and oocytes. In this paper, we have unraveled two major sites of divergence between human Bcl2l10 and its vertebrate homologs. The first one provides length variation at the N-terminus (before the BH4 domain) and the second one is located between the predicted α5-α6 pore-forming helices, providing an unprecedented case in the superfamily of helix-bundled pore-forming proteins. These two particular indels were studied phylogenetically and through biochemical and cell biological techniques, including truncation and site-directed mutagenesis. While deletion of the N-terminal extension had no significant functional impact in HeLa cells, our results suggest that the human Bcl2l10 protein evolved a calcium-binding motif in its α5-α6 interhelical region by acquiring critical negatively charged residues. Considering the reliance of female eggs on calcium-dependent proteins and calcium-regulated processes and the exceptional longevity of oocytes in the primate lineage, we propose that this microstructural variation may be an adaptive feature associated with high maternal expression of this Bcl-2 family member. |
| Databáze: | OpenAIRE |
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