| Title: | Synthesis and farnesylation of a-factor fusion proteins in Saccharomyces cerevisiae |
| Author(s): | Kolling R; Bottner B; Hollenberg CP; |
| Address: | "Institut fur Mikrobiologie, Heinrich-Heine-Universitat Dusseldorf, Germany" |
| DOI: | 10.1016/0014-5793(93)81625-a |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| Abstract: | "We have generated in-frame fusions between the mouse dihydrofolate reductase (DHFR) and parts of the a-factor MFA1 gene to explore the potential of a-factor as a secretion signal for larger polypeptides. We demonstrated that the fusion proteins are farnesylated by comparing the mobility of fusion proteins prepared from a wild-type strain and a farnesyltransferase mutant (ste16/ram1) on SDS-gels and by an in vitro farneyslation assay. In contrast to unmodified DHFR, the fusion proteins could be sedimented from cell extracts by centrifugation. Solubilization experiments indicated that the highly hydrophobic a-factor moiety renders the fusion proteins insoluble, explaining why the fusions are not secreted into the culture medium" |
| Keywords: | Amino Acid Sequence Animals Centrifugation Mating Factor Mice Molecular Sequence Data Peptides/*metabolism Protein Prenylation Recombinant Fusion Proteins/biosynthesis/isolation & purification/metabolism Saccharomyces cerevisiae/*metabolism Tetrahydrofola; |
| Notes: | "MedlineKolling, R Bottner, B Hollenberg, C P eng England 1993/12/20 FEBS Lett. 1993 Dec 20; 336(1):129-32. doi: 10.1016/0014-5793(93)81625-a" |
