Regulation of synthesis and secretion of acid and alkaline phosphatases in Neurospora crassa |
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Authors: | Sang Won Han Ely Nahas Antonio Rossi |
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Affiliation: | (1) Departamento de Quimica, FFCLRP-USP 14, 049 - Ribeirao Preto, SP, Brazil;(2) Present address: Departamento de Microbiologia, FCAVJ-UNESP, 14, 780 Jaboticabal, SP, Brazil;(3) Present address: Department of Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, Ducane Road, W12 OHS, GB London |
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Abstract: | Summary We show that N. crassa represses the production of acid phosphatase at pH higher than 8.0, irrespective of the carbon source used, whereas production was stimulated by sucrose at slightly acidic pH. The same profile of acid phosphatase production was observed in the pho-2A, pho-3A, nuc-1A, nuc-2A and pregc mutant strains. We also show that acid phosphatase synthesized by the pregc mutant strain grown on high phosphate medium has pronounced differences when compared to the enzyme synthesized by the wild-type strain grown on low phosphate medium in terms of heat stability, steady-state kinetic properties and DEAE-cellulose chromatography. In addition, the synthesis and/or secretion of only phosphate-repressible alkaline phosphatase is affected by mutations in acu-1, and acu-5 and acu-7 genes. These results, which indicate distinct pathways for the synthesis and secretion of acid and alkaline phosphatases in N. crassa, contradict the dosage titration model proposed by Metzenberg et al. (1974) whereby the synthesis of these enzymes should occur through a single hierarchical regulatory circuit as a response to phosphate starvation. |
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Keywords: | Neurospora Acid phosphatase Alkaline phosphatase Enzyme secretion |
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