Journal article
Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35
Phytochemistry (Oxford), Vol.68(11), pp.1510-1520
2007
DOI: 10.1016/j.phytochem.2007.03.021
PMID: 17466346
Abstract
The gene structure, evolutionary patterns, and organ-level expression of the 17 members of
Arabidopsis thaliana Glycoside Hydrolase Family 35 (β-galactosidases) are described. Evolutionary relationships between these and β-galactosidase genes from 22 other eukaryotes are determined. After overexpression in
Escherichia coli, homogeneous Arabidopsis BGAL4 hydrolyses chromogenic β-
d-galactosides and various β-linked galactobiosides and galactotriosides.
Catalysing the hydrolysis of terminal β-galactosyl residues from carbohydrates, galactolipids, and glycoproteins, glycoside hydrolase family 35 (β-galactosidases; BGALs) are widely distributed in plants and believed to play many key roles, including modification of cell wall components. Completion of the
Arabidopsis thaliana genome sequencing project has, for the first time, allowed an examination of the total number, gene structure, and evolutionary patterns of all Family 35 members in a representative (model) angiosperm. Reiterative database searches established a multigene family of 17 members (designated
BGAL1–
BGAL17). Using these genes as query sequences, BLAST and Hidden Markov Model searches identified
BGAL genes among 22 other eukaryotes, whose genomic sequences are known. The
Arabidopsis (
n
=
17) and rice (
n
=
15)
BGAL families were much larger than those of
Chlamydomonas, fungi, and animals (
n
=
0–4), and a lineage-specific expansion of
BGAL genes apparently occurred after divergence of the
Arabidopsis and rice lineages. All plant
BGAL genes, with the exception of
Arabidopsis BGAL17 and rice Os 9633.m04334, form a monophyletic group. Arabidopsis
BGAL expression levels are much higher in mature leaves, roots, flowers, and siliques but are lower in young seedlings.
BGAL8,
BGAL11,
BGAL13,
BGAL14, and
BGAL16 are expressed only in flowers. Catalytically active BGAL4 was produced in the
E. coli and baculoviral expression systems, purified to electrophoretic homogeneity, and partially characterized. The purified enzyme hydrolyzed
p- and
o-nitrophenyl-β-
d-galactosides. It also cleaved β-(1,3)-, β-(1,4)-, and β-(1,6)-linked galactobiosides and galactotriosides, showing a marked preference for β-(1,3)- and β-(1,4)-linkages.
Details
- Title: Subtitle
- Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35
- Creators
- Young Ock Ahn - Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USAMeiying Zheng - Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USADavid R Bevan - Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USAAsim Esen - Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USAShin-Han Shiu - Department of Plant Biology, Michigan State University, S-306 Plant Biology Building, East Lansing, MI 48824, USAJonas Benson - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USAHsiao-Ping Peng - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USAJoseph T Miller - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USAChi-Lien Cheng - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USAJonathan E Poulton - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USAMing-Che Shih - Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USA
- Resource Type
- Journal article
- Publication Details
- Phytochemistry (Oxford), Vol.68(11), pp.1510-1520
- Publisher
- Elsevier Ltd
- DOI
- 10.1016/j.phytochem.2007.03.021
- PMID
- 17466346
- ISSN
- 0031-9422
- eISSN
- 1873-3700
- Language
- English
- Date published
- 2007
- Academic Unit
- Biology
- Record Identifier
- 9984217525102771
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