Quick Search:

uzh logo
Browse by:

Zurich Open Repository and Archive

Maintenance: Tuesday, July the 26th 2016, 07:00-10:00

ZORA's new graphical user interface will be relaunched (For further infos watch out slideshow ZORA: Neues Look & Feel). There will be short interrupts on ZORA Service between 07:00am and 10:00 am. Please be patient.

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-24412

Schneider, T; Schellenberg, M; Meyer, S; Keller, F; Gehrig, P; Riedel, K; Lee, Y; Eberl, L; Martinoia, E (2009). Quantitative detection of changes in the leaf-mesophyll tonoplast proteome in dependency of a cadmium exposure of barley (Hordeum vulgare L.) plants. Proteomics, 9(10):2668-77.

Accepted Version
View at publisher
[img] PDF - Registered users only


Although the vacuole is the most important final store for toxic heavy metals like cadmium (Cd(2+)), our knowledge on how they are transported into the vacuole is still insufficient. It has been suggested that Cd(2+) can be transported as phytochelatin-Cd(2+) by an unknown ABC transporter or in exchange with protons by cation/proton exchanger (CAX) transporters. To unravel the contribution of vacuolar transporters to Cd(2+) detoxification, a quantitative proteomics approach was performed. Highly purified vacuoles were isolated from barley plants grown under minus, low (20 microM), and high (200 microM) Cd(2+ )conditions and protein levels of the obtained tonoplast samples were analyzed using isobaric tag for relative and absolute quantitation (iTRAQ). Although 56 vacuolar transporter proteins were identified, only a few were differentially expressed. Under low-Cd(2+) conditions, an inorganic pyrophosphatase and a gamma-tonoplast intrinsic protein (gamma-TIP) were up-regulated, indicating changes in energization and water fluxes. In addition, the protein ratio of a CAX1a and a natural resistance-associated macrophage protein (NRAMP), responsible for vacuolar Fe(2+) export was increased. CAX1a might play a role in vacuolar Cd(2+) transport. An increase in NRAMP activity leads to a higher cytosolic Fe(2+) concentration, which may prevent the exchange of Fe(2+) by toxic Cd(2+). Additionally, an ABC transporter homolog to AtMRP3 showed up-regulation. Under high Cd(2+) conditions, the plant response was more specific. Only a protein homologous to AtMRP3 that showed already a response under low Cd(2+) conditions, was up-regulated. Interestingly, AtMRP3 is able to partially rescue a Cd(2+)-sensitive yeast mutant. The identified transporters are good candidates for further investigation of their roles in Cd(2+) detoxification.


30 citations in Web of Science®
37 citations in Scopus®
Google Scholar™



51 downloads since deposited on 04 Dec 2009
10 downloads since 12 months

Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Functional Genomics Center Zurich
07 Faculty of Science > Department of Plant and Microbial Biology
08 University Research Priority Programs > Systems Biology / Functional Genomics
Dewey Decimal Classification:570 Life sciences; biology
580 Plants (Botany)
610 Medicine & health
Deposited On:04 Dec 2009 10:18
Last Modified:05 Apr 2016 13:34
Additional Information:Free access at DOI
Publisher DOI:10.1002/pmic.200800806
PubMed ID:19391183

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page