Ontology highlight
ABSTRACT:
SUBMITTER: Pudelski B
PROVIDER: S-EPMC3295387 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Pudelski Birgit B Schock Annette A Hoth Stefan S Radchuk Ruslana R Weber Hans H Hofmann Jörg J Sonnewald Uwe U Soll Jürgen J Philippar Katrin K
Journal of experimental botany 20111209 5
Previously, the OEP16.1 channel pore in the outer envelope membrane of mature pea (Pisum sativum) chloroplasts in vitro has been characterized to be selective for amino acids. Isolation of OEP16.2, a second OEP16 isoform from pea, in the current study allowed membrane localization and gene expression of OEP16 to be followed throughout seed development and germination of Arabidopsis thaliana and P. sativum. Thereby it can be shown on the transcript and protein level that the isoforms OEP16.1 and ...[more]