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- W137489996 abstract "Biotin levels of pea seeds were investigated in order to characterize the temporal expression of the vitamin and the pattern of protein biotinylation that can be used to define developmental stages of seed formation and germination. These studies disclosed that metabolically active and quiescent tissues can be distinguished by their biotin content. In young developing seeds, as well as in germinating seeds, there is an excess of free versus bound biotin. In young seeds biotin is bound to the housekeeping biotin enzymes. A different pattern is observed in late stages of seed formation and in mature dry seeds. Here, protein-bound biotin is in excess with respect to free biotin. This is accounted for by the accumulation of a biotinylated 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. Because the biotinylation domain of SBP65 differs markedly from that of presently known biotin enzymes, this protein defines a previously unrecognized class of biotinylated proteins. Furthermore, SBP65 shares many features in common with the LEA (Late Embryogenic Abundant) group of proteins. These results suggest that metabolic control of seed maturation and germination may occur through modulation in the level of an essential cofactor such as biotin. They also document an as yet undescribed role for some LEA proteins." @default.
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- W137489996 date "1997-01-01" @default.
- W137489996 modified "2023-09-25" @default.
- W137489996 title "The Role of Protein Biotinylation in the Development and Germination of Seeds" @default.
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- W137489996 doi "https://doi.org/10.1007/978-94-011-5716-2_4" @default.
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