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Xylose Triggers Reversible Phosphorylation of XlnR, the Fungal Transcriptional Activator of Xylanolytic and Cellulolytic Genes inAspergillus oryzae
Author(s) -
Yuji Noguchi,
Hisaki Tanaka,
Kyoko Kanamaru,
Masashi Kato,
Tetsuo Kobayashi
Publication year - 2011
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.100923
Subject(s) - phosphorylation , aspergillus oryzae , biology , xylose , transactivation , dephosphorylation , fungal protein , transcription (linguistics) , biochemistry , activator (genetics) , gene , microbiology and biotechnology , transcription factor , phosphatase , enzyme , mutant , linguistics , philosophy , fermentation
XlnR is a transcription factor that mediates D-xylose-triggered induction of xylanolytic and cellulolytic genes in Aspergillus. In order to clarify the molecular mechanisms underlying XlnR-mediated induction, Aspergillus oryzae XlnR was fused with the c-myc tag and examined by Western blotting. Phosphate-affinity SDS-PAGE revealed that XlnR was present as a mixture of variously phosphorylated forms in the absence of D-xylose, and that D-xylose triggered additional phosphorylation of the protein. D-Xylose-triggered phosphorylation was a rapid process occurring within 5 min prior to the accumulation of xynG2 mRNA, and removal of D-xylose caused slow dephosphorylation, leading to less-phosphorylated forms. At 30 min after removal, the phosphorylation status was almost identical to that in the absence of D-xylose, and the level of xynG2 mRNA started to decrease. These results indicate that XlnR is highly phosphorylated when it is active in transactivation, implying that D-xylose-triggered reversible phosphorylation controls XlnR activity.

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