Heat shock protein 90 acts in brassinosteroid signaling through interaction with BES1/BZR1 transcription factor created by Tomoaki Shigeta, Yuichi Zaizen, Yasushi Sugimoto, Yasushi Nakamura, Tomoaki Matsuo and Shigehisa Okamoto

By:

Shigeta, Tomoaki [author]

Contributor(s):

Material type: Text

TextSeries: Journal of Plant Physiology ; Volume 178Amsterdam: Elsevier GmbH, 2015Content type:

text

Media type:

unmediated

Carrier type:

volume

ISSN:

0176-1617

Subject(s):

LOC classification:

QK711.2 JOU

Online resources:

Click here to access online

Abstract: Brassinosteroids (BRs), a class of phytohormones, control various physiological and developmental processes in plants. Two highly homologous transcription factors, BRASSINOSTEROID INSENSITIVE 1-EMS-SUPRESSOR 1 (BES1) and BRASSINAZOLE RESISTANT 1 (BZR1), act downstream of BR signaling to control several thousands of putative target genes. We reported previously that BES1 forms a complex with a molecular chaperone: heat shock protein 90 (HSP90). This study demonstrates that the amino-terminal and central parts of BES1 are responsible for its physical interaction with HSP90.3 in vitro. Additionally, we present evidence that BZR1 is a novel HSP90 partner aside from two BR signaling components previously identified as its clients: BES1 and BRASSINOSTEROID INSENSITIVE 2 (BIN2). Furthermore, geldanamycin, an inhibitor of ATPase activity in HSP90, caused BES1 hyperphosphorylation and disrupted the expression of BR-responsive genes. Considered together, our results imply that HSP90 takes a part in BR-mediated gene expression through complex formation with two major transcription factors.

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Item type	Current library	Call number	Vol info	Status	Notes	Date due	Barcode
Journal Article	Main Library - Special Collections	QK711.2 JOU (Browse shelf(Opens below))	Vol. 178 (pages 69-73)	Not for loan	For in house use only

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Brassinosteroids (BRs), a class of phytohormones, control various physiological and developmental processes in plants. Two highly homologous transcription factors, BRASSINOSTEROID INSENSITIVE 1-EMS-SUPRESSOR 1 (BES1) and BRASSINAZOLE RESISTANT 1 (BZR1), act downstream of BR signaling to control several thousands of putative target genes. We reported previously that BES1 forms a complex with a molecular chaperone: heat shock protein 90 (HSP90). This study demonstrates that the amino-terminal and central parts of BES1 are responsible for its physical interaction with HSP90.3 in vitro. Additionally, we present evidence that BZR1 is a novel HSP90 partner aside from two BR signaling components previously identified as its clients: BES1 and BRASSINOSTEROID INSENSITIVE 2 (BIN2). Furthermore, geldanamycin, an inhibitor of ATPase activity in HSP90, caused BES1 hyperphosphorylation and disrupted the expression of BR-responsive genes. Considered together, our results imply that HSP90 takes a part in BR-mediated gene expression through complex formation with two major transcription factors.