Occurrence of polypeptides in other organisms cross-reacting with antibodies against A. xylinum cellulose synthase

Abstract

Antibodies (anti-83 and anti-93) against the cellulose synthase complex from A. xylinum ATCC 53582 have been employed to study the evolutionary conservation of this enzyme complex among various A. xylinum strains, selected species of other cellulose- producing bacteria, algae, and vascular plants. Of the 18 A. xylinum strains examined, the 83 Kd polypeptide clearly is detected only in 4 strains while the 93 Kd polypeptide is observed in all 18 strains. Assuming that the revised acsAB gene (Saxena et al., 1994) encoding the 83 and 93 Kd polypeptides as a single polypeptide holds true for all A. xylinum strains, it is proposed that the cellulose synthase is conserved in A. xylinum but with varying degrees of homology. An unknown regulatory mechanism causing the degradation of the 83 Kd polypeptide in response to agitated culturing conditions has been suggested to explain the absence of the 83 Kd polypeptide in most of the Acetobacter strains examined. A. xylinum cellulose synthase appears to be conserved in phylogenetically related Rhizobium and Agrobacterium species, but not in algae and plants.