PhostagTM-gel retardation and in situ thylakoid kinase assay for determination of chloroplast protein phosphorylation targets

  • The chloroplast phosphorylation network is important for posttranslational regulation of photosynthetic complexes, gene expression and metabolic pathways. In mass-spectrometric analyses a lot of putative phosphorylation targets have been found but these data need to be confirmed and brought into a physiological context. Here, we present a current protocol to quantify the phosphorylation state of thylakoid proteins and an in situ method to verify putative substrates for thylakoid associated kinases.

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Author:Yuliya Dytyuk, Falko Flügge, Olaf Czarnecki, Bernhard Grimm, Lars Dietzel
URN:urn:nbn:de:hebis:30:3-451113
URL:http://zs.thulb.uni-jena.de/receive/jportal_jparticle_00433957
Parent Title (English):Endocytobiosis and cell research
Publisher:Thüringer Univ.- und Landesbibliothek
Place of publication:Jena
Document Type:Article
Language:English
Year of Completion:2016
Date of first Publication:2016/04/21
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2017/11/30
Tag:chloroplast phosphorylation network; gel retardation; kinase protein interaction; posttranslational regulation of photosynthesis; thylakoid kinases
Volume:27
Issue:2
Page Number:9
First Page:62
Last Page:70
HeBIS-PPN:425147231
Institutes:Biowissenschaften / Biowissenschaften
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Open-Access-Publikationsfonds:Biowissenschaften
Licence (German):License LogoDeutsches Urheberrecht