Variapeptin and citropeptin were found as novel hexadepsipeptide antibiotics produced by Streptomyces variabilis and Streptomyces flavidovirens, respectively. Their structures were elucidated by NMR spectral analysis including a variety of 2D techniques. Variapeptin and citropeptin are structurally realted to azinothricin and A83586C, respectively.

The RbpA3 protein of Anabaena variabilis contains one RNA-binding domain with a carboxy-terminal glycinerich domain. Levels of two transcripts of the rbpA3 gene were differentially regulated by growth temperature. The RbpA3 protein is related to the RbpC protein within the group of cyanobacterial Rbps.

We determined the prevalence of rickettsiae in Dermacentor adults at 15 localities in Canada. Rickettsia rickettsii was not detected in any tick, whereas Rickettsia peacockii was present in 76% of Dermacentor andersoni adults and Rickettsia montanensis in 8% of Dermacentor variabilis adults. This host specificity was maintained in localities where both tick species occurred in sympatry.

A culture similar to Streptomyces variabilis was found to produce a novel cyclic hexadepsipeptide antibiotic named variapeptin. Variapeptin is structurally related to azinothricin, A83586C, and citropeptin. The antibiotic was active against Gram-positive bacteria and showed cytotoxic activity against mammalian cells.

We have determined that the type II restriction enzyme Ava II, isolated from Anabaena variabilis, recognizes and cuts the sequence (formula: see article). The eight Ava II sites of pBR322 have been mapped, as well as a unique site for Ava I.