Membrane targeting and binding of the 74-kDa form of mouse L-histidine decarboxylase via its carboxyl-terminal sequence

Sawako Suzuki, Satoshi Tanaka, Ken Ichi Nemoto, Atsushi Ichikawa

Research output: Contribution to journalArticle

25 Citations (Scopus)

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 languageEnglish
Pages (from-to)44-48
Number of pages5
JournalFEBS Letters
Volume437
Issue number1-2
DOIs
Publication statusPublished - 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

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