Abstract
The role of the C-terminal region of the 74-kDa form of l-histidine decarboxylase (HDC) in the targeting to the endoplasmic reticulum (ER) was investigated in COS-7 cells. The deletion of a 10-kDa segment (residues 578-662) of the C-terminal end of HDC, especially a 20 amino acid sequence (residues 588-607), abrogated the targeting to the ER. The C-terminal 10-kDa portion is sufficient to target the green fluorescent protein (GFP) to the ER. The 74-kDa form of HDC synthesized in an in vitro translation system post-translationally associated with the heterogeneous canine microsomal membranes. These results suggest that the C-terminal 10-kDa portion of HDC contains a signal necessary for HDC to be targeted to the ER membrane. Copyright (C) 1998 Federation of European Biochemical Societies.
Original language | English |
---|---|
Pages (from-to) | 44-48 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 437 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - Oct 16 1998 |
Keywords
- C-terminal peptide
- COS-7 cell
- Endoplasmic reticulum
- Histidine decarboxylase
- Targeting
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology