Phosphoproteomic analysis of ethylene-regulated protein phosphorylation   in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional   separations coupled with a hybrid quadrupole time-of-flight mass   spectrometer

doi:10.1002/pmic.200800420

CORC > 北京大学 > 生命科学学院

	Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer
	Li, Hao ; Wong, Wai Shing ; Zhu, Lin ; Guo, Hong Wei ; Ecker, Joseph ; Li, Ning
刊名	proteomics
	2009
关键词	Arabidopsis mutant Differential treatment Phosphoproteome Plant hormone Time-of-flight mass spectrometry Two-dimensional separations RESPONSE PATHWAY SACCHAROMYCES-CEREVISIAE MEMBRANE-PROTEINS PLASMA-MEMBRANE PLANT ETHYLENE-INSENSITIVE3 INFLORESCENCE CASCADES ENCODES KINASES
DOI	10.1002/pmic.200800420
英文摘要	Ethylene regulates a variety of stress responses and developmental adaptation in plants. In the present study, the phosphoproteomics is adopted to investigate the differential protein phosphorylation by ethylene in Arabidopsis ethylene-insensitive 2 (ein2) mutant. A total of 224 phosphopeptides were identified, of which 64 phosphopeptides were detected three or more times. Ethylene induces a general reduction in phosphorylated proteins in ein2. Totally, three ethylene-enhanced and three ethylene-repressible unique phosphopeptides were identified, respectively. Classification of the cellular functions of these phosphoproteins revealed that 55.5% of them are related to signaling and gene expression. Peptide sequence alignment reveals two highly conserved phosphorylation motifs, PRVD/G (S) under barx and (S) under bar PDYxx. Alignment of these phosphopeptides with Arabidopsis proteins reveals five phosphorylation motifs. Both ethylene-enhanced and -repressible phosphopeptides present in these motifs. EIL-1, ERF110 transcription factors and Hua enhancer 4 (HEN4) are predicted to contain one of the phosphorylation motifs. The phosphorylation of the motif-containing peptides has been validated by the in vitro kinase assays coupled with MS analysis. The differential regulation of phosphorylation by ethylene is substantiated by Western dot blot analysis. Taken together, these. results suggest that ethylene signals may be transduced by a phosphor-relay from receptors to transcriptional events via both ein2-dependent and -independent pathways.; Biochemical Research Methods; Biochemistry & Molecular Biology; SCI(E); 40; ARTICLE; 6; 1646-1661; 9
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/246491]
专题	生命科学学院
推荐引用方式 GB/T 7714	Li, Hao,Wong, Wai Shing,Zhu, Lin,et al. Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer[J]. proteomics,2009.
APA	Li, Hao,Wong, Wai Shing,Zhu, Lin,Guo, Hong Wei,Ecker, Joseph,&Li, Ning.(2009).Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer.proteomics.
MLA	Li, Hao,et al."Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer".proteomics (2009).