Dataset Information

29RNP phosphorylation site - Identification and characterization of chloroplast casein kinase II from Oryza sativa (rice)

ABSTRACT: Identfication 29RNP phosphorylation site by rice chloroplast CK2 alpha.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Oryza Sativa (rice)

SUBMITTER: Qingtao Lu

LAB HEAD: Lu Qingtao

PROVIDER: PXD000857 | Pride | 2015-04-27

REPOSITORIES: Pride

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Publications

Identification and characterization of chloroplast casein kinase II from Oryza sativa (rice).

Lu Qingtao Q Ding Shunhua S Reiland Sonja S Rödiger Anja A Roschitzki Bernd B Xue Peng P Gruissem Wilhelm W Lu Congming C Baginsky Sacha S

Journal of experimental botany 20141014 1

Plastid casein kinase II is an important regulator of transcription, posttranscriptional processes, and, most likely, different metabolic functions in dicotyledonous species. Here we report the identification and characterization of pCKII from the monocotyledonous species Oryza sativa. OspCKII activity was enriched from isolated rice chloroplasts using heparin-Sepharose chromatography, in which it co-elutes with the transcriptionally active chromosome (TAC) and several ribosomal proteins. Inclus ...[more]

PMID: 25316064

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Project description:Circadian behaviors are regulated by intrinsic biological clocks consisting of central molecular oscillators and output pathways. Despite significant progress in elucidating the central timekeeping mechanisms, the molecular pathways coupling the circadian pacemaker to overt rhythmic behavior and physiology remain elusive. The Drosophila LARK RNA-binding protein is a candidate for such a coupling factor. Previous research indicates that LARK functions downstream of the clock to mediate behavioral outputs. To better understand the roles of LARK in the Drosophila circadian system, we sought to identify RNA molecules associated with LARK in vivo, using a novel strategy that involves capturing the RNA ligands by immunoprecipitation, visualizing the captured RNAs using whole gene microarrays, and identifying functionally relevant targets through genetic screens. Experiment Overall Design: LARK-containing ribonucleoprotein complexes (LARK-RNPs) were precipitated from lysates of hand-dissected pharate adult brains using an affinity-purified anti-LARK antibody (around 1000 brains were used per immunoprecipitation experiment). A portion of each lysate was saved prior to immunoprecipitations (IPs) in order to measure the relative abundance of transcripts in a total RNA sample. RNAs extracted from the LARK-RNP and total RNA samples were labeled and hybridized to Drosophila whole-genome gene microarrays; signal intensities for individual genes were compared between samples to identify those RNAs that were enriched by immunoprecipitation (relative to their abundances in total RNA). RNAs that were selectively enriched in the LARK-RNP samples were considered to be potential targets of the RNA-binding protein. Experiment Overall Design: Due to the difficulty to dissect large amount of fly brains, only two such immunoprecipitation experiments were performed, each generating an IP RNA sample and a total RNA (control) sample. The amount of RNAs obtained from IP is very small thus only one array is used for each sample - i.e. there are only biological replicates and no technical replicate.

Dataset Information

29RNP phosphorylation site - Identification and characterization of chloroplast casein kinase II from Oryza sativa (rice)

Publications

Identification and characterization of chloroplast casein kinase II from Oryza sativa (rice).

Similar Datasets

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