Title: | Identification and structural characterization of a cDNA clone encoding a membrane-bound form of the polypeptide pheromone Er-1 in the ciliate protozoan Euplotes raikovi |
Author(s): | Miceli C; La Terza A; Bradshaw RA; Luporini P; |
Address: | "Department of Molecular, Cellular, and Animal Biology, University of Camerino, Italy" |
ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
Abstract: | "In the ciliate Euplotes raikovi, the same cell that secretes the pheromone Er-1, a polypeptide of 40 amino acids derived from a precursor (prepro-Er-1) of 75 amino acids, also produces a polypeptide of 130 amino acids, of which the 75 residues at the carboxyl terminus are identical to those of prepro-Er-1 and the 55 residues at the amino terminus form a new sequence. This larger Er-1 isoform is retained in membranes, where it may function as a binding site for soluble Er-1 in a mechanism of autocrine secretion. Membrane-bound and soluble Er-1 are translated from two mRNAs that apparently originate from a common micronuclear and/or macronuclear gene through alternative elimination of intervening sequences. This finding suggests that single genes responsible for the generation of isoform diversity in polypeptide hormones are present even in single-celled eukaryotes" |
Keywords: | "Animals Base Sequence Blotting, Western Cloning, Molecular DNA/genetics Euplotes/*genetics Gene Expression Membrane Proteins/chemistry/*genetics/immunology Molecular Sequence Data Molecular Weight Oligodeoxyribonucleotides/chemistry Pheromones/*genetics P;" |
Notes: | "MedlineMiceli, C La Terza, A Bradshaw, R A Luporini, P eng DK32465/DK/NIDDK NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1992/03/01 Proc Natl Acad Sci U S A. 1992 Mar 1; 89(5):1988-92. doi: 10.1073/pnas.89.5.1988" |