Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes - polyhedral bodies

Abstract

Carboxysomes containing the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) have been demonstrated in a variety of chemoautotrophic prokaryotes and cyanobacteria. The genes in the ccm and cso operon in Synechococcus sp. PCC7942 and Thiobacillus neapolitanus, respectively, code for several carboxysome polypeptides. The polypeptides CcmK and CsoS1 exhibit a high degree of conservation, and in turn show significant homology to the CchA and PduA polypeptides of the ethanolamine and propanediol operons of enteric bacteria. Probing Southern blots of Escherichia coli genomic DNA with csoS1A showed positive hybridization indicating the presence of a csoS1-like gene. Growing Salmonella enterica and Klebsiella oxytoca with propanediol, and E.coli with ethanolamine as the energy source under anaerobic conditions resulted in the formation of polyhedral bodies in these bacteria. The DNA - deduced amino acid sequence of three additional csoS1 genes in both Thiobacillus intermedius and Thiobacillus denitrificans was determined. The nine CsoS1 polypeptides, which includes the three previously determined for T.neapolitanus, exhibited greater than 67% sequence identity. Identity and similarity comparisons and phylogenetic analysis of known polyhedral body CsoS1-like polypeptides indicate a close structural relationship between polyhedral bodies of potentially very different function.Key words: polyhedral bodies, carboxysomes, ribulose-1,5-bisphosphate carboxylase-oxygenase, cyanobacteria, thiobacilli, enteric bacteria.