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J Bacteriol. 1972 September; 111(3): 784-790
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Changes in Activity of Glyoxylate Cycle Enzymes During Myxospore Development in Myxococcus xanthus¹

^a Department of Microbiology, Indiana University, Bloomington, Indiana 47401

ABSTRACT

Activities of the glyoxylate cycle enzymes isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2) were assayed in extracts prepared at different stages of myxospore formation in liquid cultures of Myxococcus xanthus. Activities of both enzymes attained peak values during conversion of rods to spheres. Isocitrate lyase activity decreased after reaching its peak value. Malate synthase activity also declined but at a much slower rate. The loss of isocitrate lyase activity could be prevented by the addition of chloramphenicol to cultures early in myxospore formation (during the initial rise in enzyme activity), but not by such addition at later stages of myxospore formation. The increase in glyoxylate cycle enzymes was not observed in a mutant unable to form myxospores in liquid culture under conditions suitable for morphological conversion of the wild type, or in wild-type cells incubated in the absence of an inducer for myxospore formation. It is concluded that the changes in the glyoxylate cycle enzymes represent regulatory phenomena associated with the development of the myxospore.

¹ Part of this work was presented at the Annual Meeting of the American Society for Microbiology, Philadelphia, Pa., 23–28 April 1972.

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