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The peptide HDEF as a new retention signal is necessary and sufficient to direct proteins to the endoplasmic reticulum
Author(s) -
Kaletta Karin,
Kunze Irene,
Kunze Gotthard,
Köck Margret
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01013-8
Subject(s) - endoplasmic reticulum , signal peptide , rnase p , saccharomyces cerevisiae , chitinase , vacuole , yeast , er retention , peptide , microbiology and biotechnology , biochemistry , biology , chemistry , enzyme , rna , peptide sequence , cytoplasm , gene , mutant
The key feature of tomato RNase LX localised solely outside the vacuole is the C‐terminal peptide HDEF which is very similar to known endoplasmic reticulum (ER) retention signals. For functional testing of the ER‐targeting ability of HDEF, different constructs including the complete RNase LX, two truncated forms without HDEF and the truncated chitinase FB7‐1ΔVTP C‐terminally flanked by HDEF, were expressed in Saccharomyces cerevisiae . The majority of RNase and chitinase, both containing HDEF, accumulates within the ER. However, the truncated constructs without the peptide are released into the medium. We provide compelling evidence that peptide HDEF at the C‐terminus of secretory plant proteins is a new ER retention signal in yeast and most likely in plants.