Dataset Information

Heparin_sepharose_A.thaliana - The peptide microarray "ChloroPhos1

ABSTRACT: Heparin sepharose CL-6B enrichment of lysed Arabidopsis thaliana chloroplasts was done. Elution was performed with 1M (NH4)2SO4. This elution fraction contained plastid casein kinase II activity. Their presence is proven by this multiplex MS data.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Sacha Baginsky

LAB HEAD: Sacha Baginsky

PROVIDER: PXD000981 | Pride | 2016-07-08

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	AS_20130901_HSAT_konz_001.raw.zip	Raw
	AS_20130901_HSAT_konz_001.zip	Other
	AS_20131015_HSAT_konz_002.raw.zip	Raw
	AS_20131015_HSAT_konz_002.zip	Other
	AS_20131015_HSAT_konz_003.raw.zip	Raw

Items per page:

1 - 5 of 6

Publications

The peptide microarray "ChloroPhos1.0" identifies new phosphorylation targets of plastid casein kinase II (pCKII) in Arabidopsis thaliana.

Schönberg Anna A Bergner Elena E Helm Stefan S Agne Birgit B Dünschede Beatrix B Schünemann Danja D Schutkowski Mike M Baginsky Sacha S

PloS one 20141008 10

We report the development of a peptide microarray based on previously determined phosphorylation sites in chloroplast proteins. Altogether, 905 peptides were spotted as 15mers in nine replicates onto glass slides. We used the microarray for in vitro phosphorylation experiments and specifically assessed the peptide substrate spectrum of chloroplast casein kinase II (pCKII). To this end, native pCKII from Arabidopsis thaliana and Sinapis alba chloroplasts was enriched by Heparin-Sepharose chromato ...[more]

PMID: 25295873

Similar Datasets

Project description:Plastids contain multiple copies of the plastid chromosome, folded together with proteins and RNA into nucleoids. The degree to which components of the plastid gene expression and protein biogenesis machineries are nucleoid associated, and the factors involved in plastid DNA organization, repair, and replication, are poorly understood. To provide a conceptual framework for nucleoid function, we characterized the proteomes of highly enriched nucleoid fractions of proplastids and mature chloroplasts isolated from the maize (Zea mays) leaf base and tip, respectively, using mass spectrometry. Quantitative comparisons with proteomes of unfractionated proplastids and chloroplasts facilitated the determination of nucleoid-enriched proteins. This nucleoid-enriched proteome included proteins involved in DNA replication, organization, and repair as well as transcription, mRNA processing, splicing, and editing. Many proteins of unknown function, including pentatricopeptide repeat (PPR), tetratricopeptide repeat (TPR), DnaJ, and mitochondrial transcription factor (mTERF) domain proteins, were identified. Strikingly, 70S ribosome and ribosome assembly factors were strongly overrepresented in nucleoid fractions, but protein chaperones were not. Our analysis strongly suggests that mRNA processing, splicing, and editing, as well as ribosome assembly, take place in association with the nucleoid, suggesting that these processes occur cotranscriptionally. The plastid developmental state did not dramatically change the nucleoid-enriched proteome but did quantitatively shift the predominating function from RNA metabolism in undeveloped plastids to translation and homeostasis in chloroplasts. This study extends the known maize plastid proteome by hundreds of proteins, including more than 40 PPR and mTERF domain proteins, and provides a resource for targeted studies on plastid gene expression. Details of protein identification and annotation are provided in the Plant Proteome Database.