CSM News Electronic Edition Volume 1, number 10 July 24, 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. ============== Announcements ============== David Francis would like to remind everyone that the printed/mailed version of the CSM Newsletter continues to be available. The CSM Newsletter appears every 2-3 months, and contains mainly summaries of articles which have been accepted for publication in scientific journals. It is distributed to all who wish to pay $3.00 (North American) per issue or $3.50 (overseas) per issue. Subscription invoices will be sent for 12 issues (approximately every two years). For more information contact: Angela Blaschke CSM Newsletter 657 Little Elk Creek Road Elkton, MD 21921 Phone 410-392-3920 Fax: c/o David Francis 302-831-2281 > Note: Abstracts submitted electronically to the electronic > CSM News will be automatically included in the printed CSM-Newsletter. > > Currently 62 of the 114 subscribers to the printed CSM-Newsletter > (many of them in Japan and Europe) do not subscribe to the Electronic > Edition. There are now 125 subscribers to the Electronic Edition, 73 of > whom do not get the printed version. ==================================================================== Recently Accepted Papers ==================================================================== A Developmentally Regulated Glycoprotein Complex from Dictyostelium discoideum Ned Watson1, Keith L. Williams2 and Stephen Alexander1 1 Division of Biological Sciences, University of Missouri, Columbia, MO 65211 2 School of Biological Sciences, Macquarie University, Sydney, NSW, Australia 2109 Accepted: Journal of Biological Chemistry ABSTRACT The monoclonal antibody MUD50 recognizes an epitope on a family of developmentally regulated proteins in Dictyostelium discoideum (Differentiation (1988) 38: 82-90). This epitope is an O-linked oligosaccharide which requires the wild-type modB allele for expression. These glycoproteins are structurally diverse. Some are integral membrane proteins, while others are soluble and do not require detergent for solubilization. One of the soluble glycoproteins, PsB, is also recognized by the monoclonal antibody MUD102 which binds to the polypeptide backbone. The antibody recognizes a single 100 kDa band in Western analysis. In this report we demonstrate that the PsB molecule is part of a specific developmentally regulated multiprotein complex containing 6 different proteins. The complex is held together by both covalent and non-covalent bonds. Interestingly, only the PsB glycoprotein has the MUD50 O-linked oligosaccharide determinant. None of the proteins in the complex is N-glycosylated as assessed by sensitivity to PNGase. Only one of the complex proteins is heavily phosphorylated. This work establishes the foundation for additional studies on the biosynthesis, processing and assembly of the O-glycosylated PsB protein. --------------------------------------------------------------------- [End CSM-News, volume 1, number 10]