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J Bacteriol. 1972 January; 109(1): 140-151
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Novel Mutation Causing Derepression of Several Enzymes of Sulfur Metabolism in Neurospora crassa

Earl G. Burton and Robert L. Metzenberg

Department of Physiological Chemistry, School of Medicine, University of Wisconsin, Madison, Wisconsin 53706

ABSTRACT

A group of enzymes of sulfur metabolism (arylsulfatase, cholinesulfatase, and a number of others) are normally repressed in Neurospora crassa by an abundant supply of a "favored" sulfur source such as methionine or inorganic sulfate. A mutant called sconc was isolated in which the formation of each of these enzymes is largely or completely nonrepressible. The structural genes for three of these enzymes have been mapped; sconc is not linked to any of them. It is also not linked to cys-3, another gene which is involved in control of the same group of enzymes. Two alleles of the structural gene for arylsulfatase [ars+ and ars(UFC-220)] produce electrophoretically distinguishable forms of arylsulfatase. Heterokaryons with the constitution sconc ars+ + scon+ars(UFC-220) were prepared. These heterokaryons produce both forms of arylsulfatase under conditions of sulfur limitation, but produce only the wild-type (ars+) form under conditions of sulfur abundance. When the alleles of ars and scon are in the opposite relationship, only the ars(UFC-220) form of arylsulfatase can be detected under conditions of sulfur abundance. Thus the effect of the sconc mutation seems to be limited to its own nucleus. The implications of these findings are discussed.


J Bacteriol. 1972 January; 109(1): 140-151
Copyright © 1972 American Society for Microbiology. All Rights Reserved.




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