Characterization of endoplasmic reticulum-localized UDP-D-galactose: hydroxyproline O-galactosyltransferase using synthetic peptide substrates in Arabidopsis.

Plant Physiology
Takuji OkaYoshifumi Jigami

Abstract

We characterized peptidyl hydroxyproline (Hyp) O-galactosyltransferase (HGT), which is the initial enzyme in the arabinogalactan biosynthetic pathway. An in vitro assay of HGT activity was established using chemically synthesized fluorescent peptides as acceptor substrates and extracts from Arabidopsis (Arabidopsis thaliana) T87 cells as a source of crude enzyme. The galactose residue transferred to the peptide could be detected by high-performance liquid chromatography and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry analyses. HGT required a divalent cation of manganese for maximal activity and consumed UDP-D-galactose as a sugar donor. HGT exhibited an optimal pH range of pH 7.0 to 8.0 and an optimal temperature of 35 degrees C. The favorable substrates for the activity seemed to be peptides containing two alternating imino acid residues including at least one acceptor Hyp residue, although a peptide with single Hyp residue without any other imino acids also functioned as a substrate. The results of sucrose density gradient centrifugation revealed that the cellular localization of HGT activity is identical to those of endoplasmic reticulum markers such as Sec61 and Bip, indicating that HGT is p...Continue Reading

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Citations

Apr 15, 2010·Plant Physiology·Miriam EllisAntony Bacic
Mar 20, 2016·Protoplasma·A M L van de MeeneAntony Bacic
Jan 21, 2015·The Plant Journal : for Cell and Molecular Biology·Mari Ogawa-Ohnishi, Yoshikatsu Matsubayashi
Apr 23, 2010·The Plant Journal : for Cell and Molecular Biology·Aaron H LiepmanHenrik Vibe Scheller
Jun 11, 2014·The Journal of Biological Chemistry·Fumie SaitoYoh-Ichi Shimma
Nov 30, 2019·Plant Science : an International Journal of Experimental Plant Biology·Xueyun HuRyouichi Tanaka

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