scholarly journals A rice gene encoding glycosyl hydrolase plays contrasting roles in immunity depending on the type of pathogens

2021 ◽  
Author(s):  
Chi‐Yeol Kim ◽  
Ju‐Young Park ◽  
Gobong Choi ◽  
Seongbeom Kim ◽  
Kieu Thi Xuan Vo ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Rice Gene ◽  
Gene Encoding

scholarly journals Fungal α-arabinofuranosidases of glycosyl hydrolase families 51 and 54 show a dual arabinofuranosyl- and galactofuranosyl-hydrolyzing activity

2012 ◽  
Vol 393 (8) ◽  
pp. 767-775 ◽  
Author(s):  
Boris Tefsen ◽  
Ellen L. Lagendijk ◽  
Joohae Park ◽  
Michiel Akeroyd ◽  
Doreen Schachtschabel ◽  
...  
Keyword(s):  
Cell Wall ◽  
Enzyme Activity ◽  
Molecular Modeling ◽  
Aspergillus Niger ◽  
Glycosyl Hydrolase ◽  
Hydrolase Activity ◽  
Gene Encoding ◽  
A Cell ◽  
Or Gene

Abstract Aspergillus niger possesses a galactofuranosidase activity, however, the corresponding enzyme or gene encoding this enzyme has never been identified. As evidence is mounting that enzymes exist with affinity for both arabinofuranose and galactofuranose, we investigated the possibility that α-l-arabinofuranosidases, encoded by the abfA and abfB genes, are responsible for the galactofuranosidase activity of A. niger. Characterization of the recombinant AbfA and AbfB proteins revealed that both enzymes do not only hydrolyze p-nitrophenyl-α-l-arabinofuranoside (pNp-α-Araf) but are also capable of hydrolyzing p-nitrophenyl-β-d-galactofuranoside (pNp-β-Galf). Molecular modeling of the AbfB protein with pNp-β-Galf confirmed the possibility for AbfB to interact with this substrate, similarly as with pNp-α-Araf. We also show that galactomannan, a cell wall compound of A. niger, containing β-linked terminal and internal galactofuranosyl moieties, can be degraded by an enzyme activity that is present in the supernatant of inulin-grown A. niger. Interestingly, purified AbfA and AbfB did not show this hydrolyzing activity toward A. nigergalactomannan. In summary, our studies demonstrate that AbfA and AbfB, α-l-arabinofuranosidases from different families, both contain a galactofuranose (Galf)-hydrolyzing activity. In addition, our data support the presence of a Galf-hydrolase activity expressed by A. niger that is capable of degrading fungal galactomannan.

scholarly journals Mutation of a Rice Gene Encoding a Phenylalanine Biosynthetic Enzyme Results in Accumulation of Phenylalanine and Tryptophan

2008 ◽  
Vol 20 (5) ◽  
pp. 1316-1329 ◽  
Author(s):  
Tetsuya Yamada ◽  
Fumio Matsuda ◽  
Koji Kasai ◽  
Shuichi Fukuoka ◽  
Keisuke Kitamura ◽  
...  
Keyword(s):  
Biosynthetic Enzyme ◽  
Rice Gene ◽  
Gene Encoding

OsHT, a Rice Gene Encoding for a Plasma-Membrane Localized Histidine Transporter

2005 ◽  
Vol 47 (1) ◽  
pp. 92-99 ◽  
Author(s):  
Di LIU ◽  
Wei GONG ◽  
Yong BAI ◽  
Jing-Chu LUO ◽  
Yu-Xian ZHU
Keyword(s):  
Plasma Membrane ◽  
Rice Gene ◽  
Gene Encoding

Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase

1995 ◽  
Vol 29 (3) ◽  
pp. 535-550 ◽  
Author(s):  
Qun Zhu ◽  
Tsegaye Dabi ◽  
Arlyne Beeche ◽  
Robert Yamamoto ◽  
Michael A. Lawton ◽  
...  
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Rice Gene ◽  
Gene Encoding

Overexpression of a rice gene encoding a small C2 domain protein OsSMCP1 increases tolerance to abiotic and biotic stresses in transgenic Arabidopsis

2009 ◽  
Vol 71 (4-5) ◽  
pp. 391-402 ◽  
Author(s):  
Naoki Yokotani ◽  
Takanari Ichikawa ◽  
Youichi Kondou ◽  
Satoru Maeda ◽  
Masaki Iwabuchi ◽  
...  
Keyword(s):  
Transgenic Arabidopsis ◽  
C2 Domain ◽  
Rice Gene ◽  
Gene Encoding ◽  
Abiotic And Biotic Stresses ◽  
Biotic Stresses ◽  
Domain Protein

Cloning, sequencing and overexpression of a Rhodothermus marinus gene encoding a thermostable cellulase of glycosyl hydrolase family 12

1998 ◽  
Vol 49 (3) ◽  
pp. 277-284 ◽  
Author(s):  
S. Halldórsdóttir ◽  
E. T. Thórólfsdót ◽  
R. Spilliaert ◽  
M. Johansson ◽  
S. H. Thorbjarnardóttir ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Glycosyl Hydrolase Family ◽  
Rhodothermus Marinus ◽  
Gene Encoding ◽  
Thermostable Cellulase ◽  
Hydrolase Family

scholarly journals The celA Gene, Encoding a Glycosyl Hydrolase Family 3 β-Glucosidase in Azospirillum irakense, Is Required for Optimal Growth on Cellobiosides

2001 ◽  
Vol 67 (5) ◽  
pp. 2380-2383 ◽  
Author(s):  
Denis Faure ◽  
Bernard Henrissat ◽  
David Ptacek ◽  
My Ali Bekri ◽  
Jos Vanderleyden
Keyword(s):  
Glycosyl Hydrolase ◽  
Optimal Growth ◽  
Glycosyl Hydrolase Family ◽  
Gene Encoding ◽  
Glycosyl Hydrolase Family 3 ◽  
Hydrolase Family

ABSTRACT The CelA β-glucosidase of Azospirillum irakense,belonging to glycosyl hydrolase family 3 (GHF3), preferentially hydrolyzes cellobiose and releases glucose units from the C3, C4, and C5oligosaccharides. The growth of a ΔcelA mutant on these cellobiosides was affected. In A. irakense, the GHF3 β-glucosidases appear to be functional alternatives for the GHF1 β-glucosidases in the assimilation of β-glucosides by other bacteria.

scholarly journals Streptomyces scabies 87-22 Possesses a Functional Tomatinase

2008 ◽  
Vol 190 (23) ◽  
pp. 7684-7692 ◽  
Author(s):  
Ryan F. Seipke ◽  
Rosemary Loria
Keyword(s):  
Glycosyl Hydrolase ◽  
Aerial Mycelium ◽  
Streptomyces Scabies ◽  
Wild Type ◽  
Gene Encoding ◽  
Tomato Plants ◽  
Plant Microbe Interaction ◽  
Tomato Seedlings ◽  
Disk Diffusion Assay ◽  
Potato Glycoalkaloids

ABSTRACT The actinomycete Streptomyces scabies 87-22 is the causal agent of common scab, an economically important disease of potato and taproot crops. Sequencing of the S. scabies 87-22 genome revealed the presence of a gene with high homology to the gene encoding the α-tomatine-detoxifying enzyme tomatinase found in fungal tomato pathogens. The tomA gene from S. scabies 87-22 was cotranscribed with a putative family 1 glycosyl hydrolase gene, and purified TomA protein was active only on α-tomatine and not potato glycoalkaloids or xylans. Tomatinase-null mutants were more sensitive to α-tomatine than the wild-type strain in a disk diffusion assay. Interestingly, tomatine affected only aerial mycelium and not vegetative mycelium, suggesting that the target(s) of α-tomatine is not present during vegetative growth. Severities of disease for tomato seedlings affected by S. scabies 87-22 wild-type and ΔtomA1 strains were indistinguishable, suggesting that tomatinase is not important in pathogenicity on tomato plants. However, conservation of tomA on a pathogenicity island in S. acidiscabies and S. turgidiscabies suggests a role in plant-microbe interaction.

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