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  Working day and night: Plastid casein kinase 2 catalyses phosphorylation of proteins with diverse functions in light- and dark-adapted plastids

Rödiger, A., Galonska, J., Bergner, E., Agne, B., Helm, S., Alseekh, S., et al. (2020). Working day and night: Plastid casein kinase 2 catalyses phosphorylation of proteins with diverse functions in light- and dark-adapted plastids. The Plant Journal, 104(2), 546-558. doi:10.1111/tpj.14944.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-5AC4-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-5AC5-6
Genre: Journal Article

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 Creators:
Rödiger, Anja1, Author
Galonska, Johann1, Author
Bergner, Elena1, Author
Agne, Birgit1, Author
Helm, Stefan1, Author
Alseekh, S.2, Author              
Fernie, A. R.3, Author              
Thieme, Domenika1, Author
Hoehenwarter, Wolfgang1, Author
Hause, Gerd1, Author
Pfannschmidt, Thomas1, Author
Baginsky, Sacha1, Author
Affiliations:
1External Organizations, ou_persistent22              
2The Genetics of Crop Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_3244836              
3Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              

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Free keywords: Arabidopsis thaliana, chloroplast, pCK2, phosphorylation, metabolism
 Abstract: Summary Casein kinase 2 is a ubiquitous protein kinase that has puzzled researchers for several decades because of its pleiotropic activity. Here we set out to identify the in vivo targets of plastid casein kinase 2 (pCK2) in Arabidopsis thaliana. Survey phosphoproteome analyses were combined with targeted analyses with wildtype and pck2 knockdown mutants to identify potential pCK2 targets by their decreased phosphorylation state in the mutant. To validate potential substrates, we complemented the pck2 knockdown line with TAP-tagged pCK2 and found it to restore growth parameters as well as many - but not all - putative pCK2-dependent phosphorylation events. We further performed a targeted analysis at the end-of-night to increase the specificity of target protein identification. This analysis confirmed light-independent phosphorylation of several pCK2 target proteins. Based on the aforementioned data, we define a set of in vivo pCK2-targets that span different chloroplast functions such as metabolism, transcription, translation and photosynthesis. The pleiotropy of pCK2 functions is also manifested by altered state transition kinetics during short-term-acclimation and significant alterations in the mutant metabolism supporting its function in photosynthetic regulation. Thus, our data expand our understanding on chloroplast phosphorylation networks and provide insights into kinase networks in the regulation of chloroplast functions.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1111/tpj.14944
BibTex Citekey: doi:10.1111/tpj.14944
 Degree: -

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Title: The Plant Journal
  Other : Plant J.
Source Genre: Journal
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Publ. Info: Oxford : Blackwell Science
Pages: - Volume / Issue: 104 (2) Sequence Number: - Start / End Page: 546 - 558 Identifier: ISSN: 0960-7412
CoNE: https://pure.mpg.de/cone/journals/resource/954925579095_1