Fate of highly expressed proteins destined to peroxisomes in Saccharomyces cerevisiae |
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| Authors: | A. Hartig M. Ogris G. Cohen M. Binder |
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| Affiliation: | (1) Institut für Allgemeine Biochemie der Universität Wien and Ludwig Boltzmann-Forschungsstelle für Biochemie, Währinger Strasse 38, A-1090 Wien, Austria;(2) Department of Cell Biology and Anatomy, Mount Sinai Medical Center, 1, Gustave L. Levy Place, 10029 New York, NY, USA;(3) Institut für Tumorbiologie-Krebsforschung, Borschkegasse 8a, A-1090 Wien, Austria;(4) Present address: Ernst Böhringer Institut für Arzneimittelforschung, Dr. Ernst Böhringergasse 5-11, A-1120 Wien, Austria |
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| Abstract: | ![]()
Summary Import of proteins into organelles usually requires a cis-acting targeting signal. Analysis of various hybrid proteins, consisting of mouse DHFR and parts of catalase A from Saccharomyces cerevisiae, revealed that fusion proteins containing the N-terminal 126 amino acids, or less, of catalase A remain in the cytosol whereas fusion proteins containing 140, or more, N-terminal amino acids of catalase A form large aggregates inside the cell. These protein bodies, which lack a surrounding membrane, copurified with peroxisomes on cell fractionation. The peroxisomal targeting signal of catalase A does not reside at the C-terminus or at the N-terminus.Dedicated to Prof. Dr. O. Hoffmann-Ostenhof on the occasion of his 75th birthday |
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| Keywords: | Protein translocation Saccharomyces cerevisiae Peroxisomes Overexpression |
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