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Author(s): Filosa A, English AM

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Article GUID: 11262405
Heme nitrosylation of deoxyhemoglobin by s-nitrosoglutathione requires copper.

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Article GUID: 11970954
Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana.

Author(s): Gidda SK, Miersch O, Levitin A, Schmidt J, Wasternack C, Varin L

J Biol Chem. 2003 May 16;278(20):17895-900 Authors: Gidda SK, Miersch O, Levitin A, Schmidt J, Wasternack C, Varin L

Article GUID: 12637544
The evolutionary rewiring of the ribosomal protein transcription pathway modifies the interaction of transcription factor heteromer Ifh1-Fhl1 (interacts with forkhead 1-forkhead-like 1) with the DNA-binding specificity element.

Author(s): Mallick J, Whiteway M

J Biol Chem. 2013 Jun 14;288(24):17508-19 Authors: Mallick J, Whiteway M

Article GUID: 23625919
Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates.

Author(s): Jones DR, Uddin MS, Gruninger RJ, Pham TTM, Thomas D, Boraston AB, Briggs J, Pluvinage B, McAllister TA, Forster RJ, Tsang A, Selinger LB, Abbott DW

J Biol Chem. 2017 07 28;292(30):12606-12620 Authors: Jones DR, Uddin MS, Gruninger RJ, Pham TTM, Thomas D, Boraston AB, Briggs J, Pluvinage B, McAllister TA, Forster RJ, Tsang A, Selinger LB, Abbott DW

Article GUID: 28588026
Title:Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana.
Authors:Gidda SK,  Miersch O,  Levitin A,  Schmidt J,  Wasternack C,  Varin L
Link:https://www.ncbi.nlm.nih.gov/pubmed/12637544?dopt=Abstract
DOI:10.1074/jbc.M211943200
Category:J Biol Chem
PMID:12637544
Dept Affiliation: BIOLOGY
1 Center for Structural and Functional Genomics, Biology Department, Concordia University, Montreal H3G 1M8, Canada.

Description:

Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana.

J Biol Chem. 2003 May 16;278(20):17895-900

Authors: Gidda SK, Miersch O, Levitin A, Schmidt J, Wasternack C, Varin L

Abstract

12-Hydroxyjasmonate, also known as tuberonic acid, was first isolated from Solanum tuberosum and was shown to have tuber-inducing properties. It is derived from the ubiquitously occurring jasmonic acid, an important signaling molecule mediating diverse developmental processes and plant defense responses. We report here that the gene AtST2a from Arabidopsis thaliana encodes a hydroxyjasmonate sulfotransferase. The recombinant AtST2a protein was found to exhibit strict specificity for 11- and 12-hydroxyjasmonate with K(m) values of 50 and 10 microm, respectively. Furthermore, 12-hydroxyjasmonate and its sulfonated derivative are shown to be naturally occurring in A. thaliana. The exogenous application of methyljasmonate to A. thaliana plants led to increased levels of both metabolites, whereas treatment with 12-hydroxyjasmonate led to increased level of 12-hydroxyjasmonate sulfate without affecting the endogenous level of jasmonic acid. AtST2a expression was found to be induced following treatment with methyljasmonate and 12-hydroxyjasmonate. In contrast, the expression of the methyljasmonate-responsive gene Thi2.1, a marker gene in plant defense responses, is not induced upon treatment with 12-hydroxyjasmonate indicating the existence of independent signaling pathways responding to jasmonic acid and 12-hydroxyjasmonic acid. Taken together, the results suggest that the hydroxylation and sulfonation reactions might be components of a pathway that inactivates excess jasmonic acid in plants. Alternatively, the function of AtST2a might be to control the biological activity of 12-hydroxyjasmonic acid.

PMID: 12637544 [PubMed - indexed for MEDLINE]