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PMID: 2245472 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Fate of highly expressed proteins destined to peroxisomes in Saccharomyces cerevisiae.

Current genetics ·Vol. 18 ·No. 1 ·1990-07-00 ·Pages 23-7

Hartig A, Ogris M, Cohen G, Binder M

Abstract

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.

MeSH Terms
Amino Acid Sequence Biological Transport Blotting, Western Catalase/chemistry,genetics,metabolism Cloning, Molecular Gene Expression Regulation, Fungal Immunohistochemistry Microbodies/metabolism Microscopy, Electron Molecular Sequence Data Recombinant Fusion Proteins/chemistry,genetics,metabolism Saccharomyces cerevisiae/enzymology,genetics Tetrahydrofolate Dehydrogenase/chemistry,genetics,metabolism
Chemicals
Recombinant Fusion Proteins Catalase Tetrahydrofolate Dehydrogenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hartig A
Institut für Allgemeine Biochemie, Universität Wien, Austria.
Ogris M
Cohen G
Binder M
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31 references, click to expand
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Article Info
Journal
Current genetics
Abbr.
Curr Genet
ISSN
0172-8083
DOI
10.1007/BF00321111
Published
1990-07-00
Pages
23-7
Language
English
Region
United States
NLM ID
8004904
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00321111 View journal details
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