Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme.

X. Wang, E.S. Wurtele, B.J. Nikolau

Index: Plant Physiol. 108 , 1133-1139, (1995)

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Abstract

Regulation of the expression of the gene(s) coding for the 78-kD, biotin-containing subunit of [beta]-methylcrotonyl-coenzyme A carboxylase (MCCase) was investigated in different organs of tomato (Lycopersicon esculantus) plants. The specific activity of MCCase is highest in extracts from roots, followed in descending order by ripe and ripening fruits, stems, and leaves. The specific activity is 10-fold higher in roots than in leaves. However, the steady-state levels of the 78-kD subunit of MCCase and its mRNA are approximately equal in both roots and leaves. Instead, the difference in MCCase activity between these two organs is directly correlated to the biotinylation status of the enzyme's biotin-containing subunit. Thus, the lower activity of MCCase in leaves is attributed to the reduced biotinylation of the biotin-containing subunit of the enzyme. Consistent with this model, a pool of nonbiotinylated enzyme is present in leaves, whereas the nonbiotinylated enzyme is undetectable in roots. The underbiotinylation of MCCase in leaves is not due to a lack of biotin in this organ, since the biotin concentration is 4- to 5-fold higher in leaves than in roots. These observations indicate that the posttranslational biotinylation of the biotin-containing sub-unit of MCCase is an important mechanism for regulating the organ-specific expression of MCCase activity.