TY  - JOUR
A1  - Dytyuk, Yuliya
A1  - Flügge, Falko
A1  - Czarnecki, Olaf
A1  - Grimm, Bernhard
A1  - Dietzel, Lars
T1  - PhostagTM-gel retardation and in situ thylakoid kinase assay for determination of chloroplast protein phosphorylation targets
T2  - Endocytobiosis and cell research
N2  - 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.
KW  - chloroplast phosphorylation network
KW  - posttranslational regulation of photosynthesis
KW  - thylakoid kinases
KW  - gel retardation
KW  - kinase protein interaction
Y1  - 2016
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/45111
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-451113
UR  - http://zs.thulb.uni-jena.de/receive/jportal_jparticle_00433957
VL  - 27
IS  - 2
SP  - 62
EP  - 70
PB  - Thüringer Univ.- und Landesbibliothek
CY  - Jena
ER  -