CSM News Electronic Edition Volume 1, number 21 November 13, 1993 Please submit abstracts of your papers as soon as they have been accepted for publication by sending them to CSM-News@worms.cmsbio.nwu.edu. Back issues of CSM-News, the CSM Reference database and other useful information is available by anonymous ftp from worms.cmsbio.nwu.edu [129.105.233.50]. ============ Announcement ============ Back issues of the CSM-News, the Franke Reference Database, Rich Sucgang's Dicty Gene Disruption Table and everything else in the CSM Archive are now available through a new Gopher server as well as the World Wide Web. If you don't know about the World Wide Web and are interested in Electronic Communication it is worth finding out about it. If you have a network connection a single client program called mosaic (which exists in versions that run on PCs or Macs or pretty much any unix machine) will let you connect to virtually any ftp server, gopher server, telnet site or world wide web site. The advantage is that you can read documents (such as the back issues of the CSM-News) on line. In addition, the clients also display graphics. The main site for Mosaic and information about WWW is ftp.ncsa.uiuc.edu. The clients are available from that site. To use gopher to connect the the CSM Server point your Gopher client to "worms.cmsbio.nwu.edu", port 70. You can also point your Mosaic client to "http://www.acns.nwu.edu/" and select "CSM Gopher". =========== ABSTRACTS =========== A calcium and calmodulin-dependent protein kinase present in differentiating Dictyostelium discoideum Andrew J.Dunbar and John F. Wheldrake. FEMS Micro. Lett., in press. A protein kinase from Dictyostelium discoideum which phosphorylates the synthetic peptide, calmodulin-dependent protein kinase substrate (sequence PLRRTLSVAA) and is stimulated by calcium/calmodulin is described. This is the first report of a protein kinase with these characteristics in Dictyostelium discoideum. The enzyme was partially purified by Q-Sepharose chromatography. The protein kinase is very labile, and rapidly loses calcium/calmodulin-dependence upon standing at 4 degrees even in the presence of protease inhibitors, making further purification and characterisation difficult. In the active fractions, a 55kDa polypeptide is labelled with gamma 32P ATP in vitro under conditions in which intramolecular rather than intermolecular reactions are favoured. The phosphorylation of this peptide is stimulated in the presence of calcium and calmodulin but not calcium alone. Calcium/calmodulin-dependent stimulation is inhibited in the presence of the calmodulin antagonist, trifluoperazine. It is proposed that the 55kDa polypeptide may represent the autophosphorylated form of the enzyme. ---------------------------------------------------------------------- [[END CSM-News, volume 1, number 21]]