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The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site

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Abstract

Seeds of Pisum sativum contain a biotinyl polypeptide called SBP65 that behaves as a putative sink for the free vitamin, representing more than 90% of the total protein-bound biotin in mature seeds. A cDNA encoding SBP65 was cloned and sequenced. The deduced primary structure of the protein was confirmed by protein sequencing. Peptide sequencing also indicated binding of the biotin to lysine 103. The biotinylation domain of SBP65 differs markedly from that of presently known biotin enzymes. Molecular analysis of the protein sequence reveals an extremely hydrophilic protein containing several repeated motifs. These properties, as well as the temporal and spatial patterns of expression of this protein, suggest that SBP65 belongs to the LEA (late embryogenesis-abundant) group of proteins.

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Authors and Affiliations

  1. Laboratoire Mixte CNRS/Rhône-Poulenc (UM41 associée au Centre National de la Recherche Scientifique), Rhône-Poulenc Agrochimie, 14-20 rue Pierre Baizet, 69263, Lyon cedex 9, France

    Manuel Duval, Claudette Job, Roland Douce & Dominique Job

  2. Laboratoire de Biochimie Moléculaire et de Biologie Cellulaire, Rhône-Poulenc Agrochimie, 14-20 rue Pierre Baizet, 69263, Lyon cedex 9, France

    Richard T. DeRose

  3. Département des Biotechnologies, Rhône-Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, 13 quai Jules Guesdes, B.P. 14, 94403, Vitry sur Seine cedex, France

    Didier Faucher

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  1. Manuel Duval
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  2. Richard T. DeRose
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  3. Claudette Job
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  4. Didier Faucher
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  5. Roland Douce
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  6. Dominique Job
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Duval, M., DeRose, R.T., Job, C. et al. The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site. Plant Mol Biol 26, 265–273 (1994). https://doi.org/10.1007/BF00039537

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  • DOI: https://doi.org/10.1007/BF00039537

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