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

Michael Orlowski, Presley Martin, David White, Michael Chi-Wai Wong
1972 Journal of Bacteriology  
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
more » ... 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. MATERIALS AND METHODS Organism. M. xanthus, strain FB (9), and a mutant (designated GNI) derived from FB were used. 784 on May 9, 2020 by guest
doi:10.1128/jb.111.3.784-790.1972 fatcat:z5rm4bkrdfbxjirluu6wg2k5au