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1.
Plant J ; 82(4): 621-31, 2015 May.
Artigo em Inglês | MEDLINE | ID: mdl-25823965

RESUMO

Long terminal repeat retrotransposons (LTR-RTs) represent a major fraction of plant genomes, but processes leading to transposition bursts remain elusive. Polyploidy expectedly leads to LTR-RT proliferation, as the merging of divergent diploids provokes a genome shock activating LTR-RTs and/or genetic redundancy supports the accumulation of active LTR-RTs through relaxation of selective constraints. Available evidence supports interspecific hybridization as the main trigger of genome dynamics, but few studies have addressed the consequences of intraspecific polyploidy (i.e. autopolyploidy), where the genome shock is expectedly minimized. The dynamics of LTR-RTs was thus here evaluated through low coverage 454 sequencing of three closely related diploid progenitors and three independent autotetraploids from the young Biscutella laevigata species complex. Genomes from this early diverging Brassicaceae lineage presented a minimum of 40% repeats and a large diversity of transposable elements. Differential abundances and patterns of sequence divergence among genomes for 37 LTR-RT families revealed contrasted dynamics during species diversification. Quiescent LTR-RT families with limited genetic variation among genomes were distinguished from active families (37.8%) having proliferated in specific taxa. Specific families proliferated in autopolyploids only, but most transpositionally active families in polyploids were also differentiated among diploids. Low expression levels of transpositionally active LTR-RT families in autopolyploids further supported that genome shock and redundancy are non-mutually exclusive triggers of LTR-RT proliferation. Although reputed stable, autopolyploid genomes show LTR-RT fractions presenting analogies with polyploids between widely divergent genomes.


Assuntos
Mostardeira/genética , Retroelementos/genética , Evolução Molecular , Genoma de Planta/genética , Dados de Sequência Molecular , Filogenia , Poliploidia , Sequências Repetidas Terminais/genética
2.
Proc Natl Acad Sci U S A ; 109(51): 20986-91, 2012 Dec 18.
Artigo em Inglês | MEDLINE | ID: mdl-23213212

RESUMO

Mollusca evolutionary success can be attributed partly to their efficiency to sustain and protect their soft body with an external biomineralized structure, the shell. Current knowledge of the protein set responsible for the formation of the shell microstructural polymorphism and unique properties remains largely patchy. In Pinctada margaritifera and Pinctada maxima, we identified 80 shell matrix proteins, among which 66 are entirely unique. This is the only description of the whole "biomineralization toolkit" of the matrices that, at least in part, is thought to regulate the formation of the prismatic and nacreous shell layers in the pearl oysters. We unambiguously demonstrate that prisms and nacre are assembled from very different protein repertoires. This suggests that these layers do not derive from each other.


Assuntos
Regulação da Expressão Gênica , Pinctada/fisiologia , Animais , Evolução Biológica , Carbonato de Cálcio/química , Evolução Molecular , Imuno-Histoquímica , Dados de Sequência Molecular , Moluscos/fisiologia , Nácar/metabolismo , Pinctada/química , Estrutura Terciária de Proteína , Proteoma , Proteômica/métodos , Transcrição Gênica , Transcriptoma
3.
Amino Acids ; 42(5): 2009-17, 2012 May.
Artigo em Inglês | MEDLINE | ID: mdl-21590302

RESUMO

Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO3 and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those of the other nacre proteins already described. This unusual methionine-rich protein is a new member in the growing list of low complexity domain containing proteins that are associated with biocalcifications. These observations offer new insights to the molecular mechanisms of biomineralization.


Assuntos
Calcificação Fisiológica , Metionina , Pinctada , Proteínas/isolamento & purificação , Sequência de Aminoácidos , Animais , Células Epiteliais/química , Expressão Gênica , Metionina/química , Dados de Sequência Molecular , Nácar/química , Pinctada/química , Estrutura Terciária de Proteína , Proteínas/química , Proteínas/genética
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