ISSN:
1432-0983
Keywords:
Protein translocation
;
Saccharomyces cerevisiae
;
Peroxisomes
;
Overexpression
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00321111
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