The EMBO Journal
 
Advanced search
Journal home
Current issue
Advance Online Publication
Web Focuses
Archive
Browse by subject
Free online sample issue
Aims and scope
Press releases
ToC by email
Authors & Referees
Guide for authors
Submit an Article
Guide for referees
Editorial Team, Senior Advisors and Advisory Editorial Board
Contact Editorial office
Customer services
Subscribe
Order sample copy
Purchase articles
Reprints and permissions
Contact NPG
Advertising
EMBO
www.embo.org
Article
Subject Categories: Membranes & Transport | Plant Biology
The EMBO Journal (2007) 26, 3203–3215, doi:10.1038/sj.emboj.7601757
Published online 14 June 2007
An Arabidopsis quiescin-sulfhydryl oxidase regulates cation homeostasis at the root symplast–xylem interface
Santiago Alejandro1, Pedro L Rodríguez1, Jose M Bellés1, Lynne Yenush1, María J García-Sanchez2, José A Fernández2 and Ramón Serrano1
1 Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-CSIC, Camino de Vera s/n, Valencia, Spain
2 Departamento de Biología Vegetal, Facultad de Ciencias, Universidad de Málaga, Campus de Teatinos, Málaga, Spain

To whom correspondence should be addressed
Ramón Serrano, Instituto de Biología Molecular y Celular de Plantas, Universidad Politecnica de Valencia-CSIC, Camino de Vera s/n, Valencia 46022, Spain. Tel.: +34 96 387 7883; Fax: +34 96 387 7859; E-mail: rserrano@ibmcp.upv.es

Received 22 January 2007; Accepted 18 May 2007; Published online 14 June 2007.
Abstract
A genetic screen of Arabidopsis 'activation-tagging' mutant collection based on tolerance to norspermidine resulted in a dominant mutant (par1-1D) with increased expression of the QSO2 gene (At1g15020), encoding a member of the quiescin-sulfhydryl oxidase (QSO) family. The par1-1D mutant and transgenic plants overexpressing QSO2 cDNA grow better than wild-type Arabidopsis in media with toxic cations (polyamines, Li+ and Na+) or reduced K+ concentrations. This correlates with a decrease in the accumulation of toxic cations and an increase in the accumulation of K+ in xylem sap and shoots. Conversely, three independent loss-of-function mutants of QSO2 exhibit phenotypes opposite to those of par1-1D. QSO2 is mostly expressed in roots and is upregulated by K+ starvation. A QSO2double colonGFP fusion ectopically expressed in leaf epidermis localized at the cell wall. The recombinant QSO2 protein, produced in yeast in secreted form, exhibits disulfhydryl oxidase activity. A plausible mechanism of QSO2 action consists on the activation of root systems loading K+ into xylem, but different from the SKOR channel, which is not required for QSO2 action. These results uncover QSOs as novel regulators of ion homeostasis.
Keywords: activation-tagging, K+ transport, salinity, red-ox regulation
Send to a friendEmail link to a friend
PDFDownload PDF
Full textFull text
Next article
Previous article
Table of contents
rights and permissionsRights and permissions
order commercial reprintsReprints
ToC alertRegister for table of contents by email
  Privacy policy Copyright © 2007 by the European Molecular Biology Organization