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J Biol Chem, Vol. 274, Issue 52, 37321-37328, December 24, 1999

Structure and Regulated Expression of the -Aminolevulinate Synthase Gene from Drosophila melanogaster^*

Inmaculada Ruiz de Mena^§, Miguel A. Fernández-Moreno, Belén Bornstein, Laurie S. Kaguni^§, and Rafael Garesse^¶

From the  Departamento de Bioquímica, UAM, Instituto de Investigaciones Biomédicas "Alberto Sols" CSIC-UAM Facultad de Medicina, Universidad Autónoma de Madrid c/Arzobispo Morcillo 4, 28029 Madrid, Spain and the ^§ Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824-1319

The structure of the single copy gene encoding the putative housekeeping isoform of Drosophila melanogaster -aminolevulinate synthase (ALAS) has been determined. Southern and immunoblot analyses suggest that only the housekeeping isoform of the enzyme exists in Drosophila. We have localized a critical region for promoter activity to a sequence of 121 base pairs that contains a motif that is potentially recognized by factors of the nuclear respiratory factor-1 (NRF-1)/P3A2 family, flanked by two AP4 sites. Heme inhibits the expression of the gene by blocking the interaction of putative regulatory proteins to its 5' proximal region, a mechanism different from those proposed for other hemin-regulated promoters. Northern and in situ RNA hybridization experiments show that maternal alas mRNA is stored in the egg; its steady-state level decreases rapidly during the first hours of development and increases again after gastrulation in a period where the synthesis of several mRNAs encoding metabolic enzymes is activated. In the syncytial blastoderm, the alas mRNA is ubiquitously distributed and decreases in abundance substantially through cellular blastoderm. Late in embryonic development alas shows a specific pattern of expression, with an elevated mRNA level in oenocytes, suggesting an important role of these cells in the biosynthesis of hemoproteins in Drosophila.

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