Return to search

Isolation and characterization of Dictyostelium discoideum genes encoding a common proline-rich region

CABP1 is a cAMP-binding protein found in Dictyostelium discoideum. Anti-CABP1 monoclonal antibody cross-reacts with several polypeptides. The gene encoding CABP1, capA, cross-hybridizes to seven genomic fragments on a genomic DNA Southern blot. Clones representing four different capA-related sequences were obtained by screening both cDNA and genomic libraries with the anti-CABP1 monoclonal antibody and with a capA cDNA. Sequence analysis revealed that the structural similarities between CABP1 and two CABP1-related polypeptides are restricted to a region highly enriched for proline, glycine, glutamine, and tyrosine residues. One of these capA-related sequences encodes the p24 actin-binding protein and the other encodes a homologue of human annexin VII. The levels of the p24 transcript were found to decrease in response to the addition of extracellular cAMP and to increase in the presence of the protein synthesis inhibitor cycloheximide. As a preliminary step towards understanding the function of annexin VII, specific antibodies were generated. Immunoblot analysis revealed the existence of two polypeptides with sizes expected for the two products of the alternatively spliced annexin VII encoding gene.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.39517
Date January 1992
CreatorsGreenwood, Michael T.
ContributorsTsang, A. (advisor), Lasko, P. (advisor)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageDoctor of Philosophy (Department of Biology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001324550, proquestno: NN87612, Theses scanned by UMI/ProQuest.

Page generated in 0.0021 seconds