Membrane targeting and binding of the 74-kDa form of mouse L-histidine decarboxylase via its carboxyl-terminal sequence.
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.
Suzuki
S
S
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Tanaka
S
S
Nemoto
K
K
Ichikawa
A
A
D000818:Animals; D019556:COS Cells; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006640:Histidine Decarboxylase / Q000737:chemistry / Q000378:metabolism*; D015151:Immunoblotting; D007425:Intracellular Membranes / Q000378:metabolism*; D051379:Mice; D018613:Microscopy, Confocal; D016296:Mutagenesis; D014176:Protein Biosynthesis; D014158:Transcription, Genetic; D014162:Transfection
D006640:Histidine Decarboxylase