Genetics, Vol. 156, 1559-1571, December 2000, Copyright © 2000

The Aspergillus nidulans xprF Gene Encodes a Hexokinase-like Protein Involved in the Regulation of Extracellular Proteases

Margaret E. Katza, Amir Masoumia, Stephen R. Burrowsa, Carolyn G. Shirtliffa, and Brian F. Cheethama
a Molecular and Cellular Biology Division, School of Biological Sciences, University of New England, Armidale, New South Wales 2351, Australia

Corresponding author: Margaret E. Katz, School of Biological Sciences, University of New England, Armidale, NSW 2351, Australia., mkatz{at}metz.une.edu.au (E-mail)

Communicating editor: M. HAMPSEY

The extracellular proteases of Aspergillus nidulans are produced in response to limitation of carbon, nitrogen, or sulfur, even in the absence of exogenous protein. Mutations in the A. nidulans xprF and xprG genes have been shown to result in elevated levels of extracellular protease in response to carbon limitation. The xprF gene was isolated and sequence analysis indicates that it encodes a 615-amino-acid protein, which represents a new type of fungal hexokinase or hexokinase-like protein. In addition to their catalytic role, hexokinases are thought to be involved in triggering carbon catabolite repression. Sequence analysis of the xprF1 and xprF2 alleles showed that both alleles contain nonsense mutations. No loss of glucose or fructose phosphorylating activity was detected in xprF1 or xprF2 mutants. There are two possible explanations for this observation: (1) the xprF gene may encode a minor hexokinase or (2) the xprF gene may encode a protein with no hexose phosphorylating activity. Genetic evidence suggests that the xprF and xprG genes are involved in the same regulatory pathway. Support for this hypothesis was provided by the identification of a new class of xprG- mutation that suppresses the xprF1 mutation and results in a protease-deficient phenotype.





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