scholarly journals Genome-Wide Analysis of Glycoside Hydrolase Family 1 β-glucosidase Genes in Brassica rapa and Their Potential Role in Pollen Development

2019 ◽  
Vol 20 (7) ◽  
pp. 1663 ◽  
Author(s):  
Xiangshu Dong ◽  
Yuan Jiang ◽  
Yoonkang Hur
Keyword(s):  
Stress Responses ◽  
Pollen Development ◽  
Glycoside Hydrolase ◽  
Brassica Species ◽  
Glycoside Hydrolase Family ◽  
Vegetable Crops ◽  
Genome Wide ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family ◽  
Tandem Duplications

Glycoside hydrolase family 1 (GH1) β-glucosidases (BGLUs) are encoded by a large number of genes, and are involved in many developmental processes and stress responses in plants. Due to their importance in plant growth and development, genome-wide analyses have been conducted in model plants (Arabidopsis and rice) and maize, but not in Brassica species, which are important vegetable crops. In this study, we systematically analyzed B. rapa BGLUs (BrBGLUs), and demonstrated the involvement of several genes in pollen development. Sixty-four BrBGLUs were identified in Brassica databases, which were anchored onto 10 chromosomes, with 10 tandem duplications. Phylogenetic analysis revealed that 64 genes were classified into 10 subgroups, and each subgroup had relatively conserved intron/exon structures. Clustering with Arabidopsis BGLUs (AtBGLUs) facilitated the identification of several important subgroups for flavonoid metabolism, the production of glucosinolates, the regulation of abscisic acid (ABA) levels, and other defense-related compounds. At least six BrBGLUs might be involved in pollen development. The expression of BrBGLU10/AtBGLU20, the analysis of co-expressed genes, and the examination of knocked down Arabidopsis plants strongly suggests that BrBGLU10/AtBGLU20 has an indispensable function in pollen development. The results that are obtained from this study may provide valuable information for the further understanding of β-glucosidase function and Brassica breeding, for nutraceuticals-rich Brassica crops.

Cloning and characterization of a novel cellobiase gene, cba3, encoding the first known β-glucosidase of glycoside hydrolase family 1 of Cellulomonas biazotea

Gene ◽  
2012 ◽  
Vol 493 (1) ◽  
pp. 52-61 ◽  
Author(s):  
Anthony K.N. Chan ◽  
Yule Y. Wang ◽  
K.L. Ng ◽  
Zhibiao Fu ◽  
W.K.R. Wong
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Cellulomonas Biazotea ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Substrate specificity of glycoside hydrolase family 1 β-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism

2021 ◽  
Author(s):  
Shu Horikoshi ◽  
Wataru Saburi ◽  
Jian Yu ◽  
Hideyuki Matsuura ◽  
James R Ketudat Cairns ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Glycoside Hydrolase ◽  
Sequence Similarity ◽  
Glycoside Hydrolase Family ◽  
Its Sequence ◽  
Cell Wall Metabolism ◽  
Bioactive Substances ◽  
Chain Length Specificity ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

ABSTRACT Plants possess many glycoside hydrolase family 1 (GH1) β-glucosidases, which physiologically function in cell wall metabolism and activation of bioactive substances, but most remain uncharacterized. One GH1 isoenzyme AtBGlu42 in Arabidopsis thaliana has been identified to hydrolyze scopolin using the gene deficient plants, but no enzymatic properties were obtained. Its sequence similarity to another functionally characterized enzyme Os1BGlu4 in rice suggests that AtBGlu42 also acts on oligosaccharides. Here, we show that the recombinant AtBGlu42 possesses high kcat/Km not only on scopolin, but also on various β-glucosides, cellooligosaccharides, and laminarioligosaccharides. Of the cellooligosaccharides, cellotriose was the most preferred. The crystal structure, determined at 1.7 Å resolution, suggests that Arg342 gives unfavorable binding to cellooligosaccharides at subsite +3. The mutants R342Y and R342A showed the highest preference on cellotetraose or cellopentaose with increased affinities at subsite +3, indicating that the residues at this position have an important role for chain length specificity.

scholarly journals Sphingadienine-1-phosphate levels are regulated by a novel glycoside hydrolase family 1 glucocerebrosidase widely distributed in seed plants

2021 ◽  
pp. 101236
Author(s):  
Jinichiro Koga ◽  
Makoto Yazawa ◽  
Koji Miyamoto ◽  
Emi Yumoto ◽  
Tomoyoshi Kubota ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Seed Plants ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

scholarly journals Protein-carbohydrate Interactions Leading to Hydrolysis and Transglycosylation in Plant Glycoside Hydrolase Family 1 Enzymes

2012 ◽  
Vol 59 (2) ◽  
pp. 51-62 ◽  
Author(s):  
James R. Ketudat Cairns ◽  
Salila Pengthaisong ◽  
Sukanya Luang ◽  
Sompong Sansenya ◽  
Anupong Tankrathok ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1

2004 ◽  
Vol 55 (3) ◽  
pp. 343-367 ◽  
Author(s):  
Zhiwei Xu ◽  
Luis Escamilla-Trevi�o ◽  
Lihui Zeng ◽  
Mallikarjun Lalgondar ◽  
David Bevan ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Glycoside Hydrolase ◽  
Genomic Analysis ◽  
Glycoside Hydrolase Family ◽  
Functional Genomic ◽  
Functional Genomic Analysis ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Motif-Guided Identification of a Glycoside Hydrolase Family 1 α-L-Arabinofuranosidase inBifidobacterium adolescentis

2013 ◽  
Vol 77 (8) ◽  
pp. 1709-1714 ◽  
Author(s):  
Hirokazu SUZUKI ◽  
Ayano MURAKAMI ◽  
Ken-ichi YOSHIDA
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family
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