Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum

Koji Yuasa, Kiminori Toyooka, Hiroo Fukuda, Ken Matsuoka

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

We cloned a novel prolyl 4-hydroxylase (PH; EC 1.14.11.2) homolog cDNA from tobacco (Nicotiana tabacum) BY-2 cells based on expression sequence tag information. Like other PHs, this tobacco PH polypeptide has two conserved histidine residues, and it comprises 286 amino acids with a calculated molecular mass of 32 kDa. Interestingly, this protein and homologs in Arabidopsis and rice have predicted transmembrane sequences in their N-terminal regions. This PH homolog was expressed in BY-2 cells as a His-tagged protein, and the expressed protein showed PH activity. Incubation of membranes with high salt, urea, and protease with or without detergents indicated that this protein is an integral membrane protein with a type II configuration. Its membrane-anchored nature is specific for plants because no integral membrane PH has been found in animals. A membrane fractionation study and immunocytochemical studies indicate that this protein localizes in both the endoplasmic reticulum (ER) and Golgi apparatus. Analysis of this protein fused to green fluorescent protein indicated that basic amino acids in the cytoplasmic, N-terminal region of the PH play a role in its export from the ER.

Original languageEnglish
Pages (from-to)81-94
Number of pages14
JournalPlant Journal
Volume41
Issue number1
DOIs
Publication statusPublished - Jan 1 2005
Externally publishedYes

Fingerprint

procollagen-proline dioxygenase
Prolyl Hydroxylases
Endoplasmic Reticulum
endoplasmic reticulum
Membranes
Tobacco
Proteins
proteins
tobacco
Basic Amino Acids
amino acids
Golgi Apparatus
Golgi apparatus
Green Fluorescent Proteins
green fluorescent protein
histidine
Arabidopsis
Histidine
membrane proteins
detergents

All Science Journal Classification (ASJC) codes

  • Genetics
  • Plant Science
  • Cell Biology

Cite this

Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. / Yuasa, Koji; Toyooka, Kiminori; Fukuda, Hiroo; Matsuoka, Ken.

In: Plant Journal, Vol. 41, No. 1, 01.01.2005, p. 81-94.

Research output: Contribution to journalArticle

Yuasa, Koji ; Toyooka, Kiminori ; Fukuda, Hiroo ; Matsuoka, Ken. / Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. In: Plant Journal. 2005 ; Vol. 41, No. 1. pp. 81-94.
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