Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans

Md Ziaur Rahman, Megumi Maeda, Satsuki Itano, Md Anowar Hossain, Takeshi Ishimizu, Yoshinobu Kimura

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568 or Solyc03g006980, α-Fuc'ase S1-1), which may be involved in the turnover of plant complex-type N-glycans. Recombinant α-Fuc'ase S1-1 (rFuc'ase S1-1) was expressed using a baculovirus-insect cell expression system. rFuc'ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Lea epitopes on plant complex-type N-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-type N-glycans. Molecular 3D modelling of α-Fuc'ase Sl-1 and structure/sequence interpretation based on comparison with a homologous a-fucosidase from Bifidobacterium longum subsp. infantis (Blon-2336) indicated that residues Asp193 and Glu237 might be important for substrate binding.

Original languageEnglish
Pages (from-to)421-432
Number of pages12
JournalJournal of Biochemistry
Volume161
Issue number5
DOIs
Publication statusPublished - May 1 2017

Fingerprint

alpha-L-Fucosidase
Fucose
Hydrolases
Lycopersicon esculentum
Polysaccharides
Degradation
Rubiaceae
Baculoviridae
Oligosaccharides
Insects
Epitopes
Genes
Substrates

Keywords

  • A-fucosidase
  • Plant glycoprotein
  • Plant N-glycan
  • Solanum lycopersicum
  • Tomato

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Molecular Biology

Cite this

Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans. / Rahman, Md Ziaur; Maeda, Megumi; Itano, Satsuki; Hossain, Md Anowar; Ishimizu, Takeshi; Kimura, Yoshinobu.

In: Journal of Biochemistry, Vol. 161, No. 5, 01.05.2017, p. 421-432.

Research output: Contribution to journalArticle

@article{eea4471f8f63424f88cf8a8199af4234,
title = "Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans",
abstract = "In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568 or Solyc03g006980, α-Fuc'ase S1-1), which may be involved in the turnover of plant complex-type N-glycans. Recombinant α-Fuc'ase S1-1 (rFuc'ase S1-1) was expressed using a baculovirus-insect cell expression system. rFuc'ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Lea epitopes on plant complex-type N-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-type N-glycans. Molecular 3D modelling of α-Fuc'ase Sl-1 and structure/sequence interpretation based on comparison with a homologous a-fucosidase from Bifidobacterium longum subsp. infantis (Blon-2336) indicated that residues Asp193 and Glu237 might be important for substrate binding.",
keywords = "A-fucosidase, Plant glycoprotein, Plant N-glycan, Solanum lycopersicum, Tomato",
author = "Rahman, {Md Ziaur} and Megumi Maeda and Satsuki Itano and Hossain, {Md Anowar} and Takeshi Ishimizu and Yoshinobu Kimura",
year = "2017",
month = "5",
day = "1",
doi = "10.1093/jb/mvw089",
language = "English",
volume = "161",
pages = "421--432",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "5",

}

TY - JOUR

T1 - Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans

AU - Rahman, Md Ziaur

AU - Maeda, Megumi

AU - Itano, Satsuki

AU - Hossain, Md Anowar

AU - Ishimizu, Takeshi

AU - Kimura, Yoshinobu

PY - 2017/5/1

Y1 - 2017/5/1

N2 - In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568 or Solyc03g006980, α-Fuc'ase S1-1), which may be involved in the turnover of plant complex-type N-glycans. Recombinant α-Fuc'ase S1-1 (rFuc'ase S1-1) was expressed using a baculovirus-insect cell expression system. rFuc'ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Lea epitopes on plant complex-type N-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-type N-glycans. Molecular 3D modelling of α-Fuc'ase Sl-1 and structure/sequence interpretation based on comparison with a homologous a-fucosidase from Bifidobacterium longum subsp. infantis (Blon-2336) indicated that residues Asp193 and Glu237 might be important for substrate binding.

AB - In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568 or Solyc03g006980, α-Fuc'ase S1-1), which may be involved in the turnover of plant complex-type N-glycans. Recombinant α-Fuc'ase S1-1 (rFuc'ase S1-1) was expressed using a baculovirus-insect cell expression system. rFuc'ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Lea epitopes on plant complex-type N-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-type N-glycans. Molecular 3D modelling of α-Fuc'ase Sl-1 and structure/sequence interpretation based on comparison with a homologous a-fucosidase from Bifidobacterium longum subsp. infantis (Blon-2336) indicated that residues Asp193 and Glu237 might be important for substrate binding.

KW - A-fucosidase

KW - Plant glycoprotein

KW - Plant N-glycan

KW - Solanum lycopersicum

KW - Tomato

UR - http://www.scopus.com/inward/record.url?scp=85019709539&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85019709539&partnerID=8YFLogxK

U2 - 10.1093/jb/mvw089

DO - 10.1093/jb/mvw089

M3 - Article

C2 - 28039392

AN - SCOPUS:85019709539

VL - 161

SP - 421

EP - 432

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 5

ER -