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MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.

Published bySuparman Iskandar Modified over 5 years ago

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Presentation on theme: "MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins."— Presentation transcript:

1 MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.
MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins. The 28-kDa band from root PM enriched in hydrophobic proteins was digested by Lys-C. Phosphopeptides were enriched using a TiO2 column. All C-terminal phosphopeptides expected from root AtPIP aquaporins cannot be simultaneously recorded onto the same MS spectrum. The present spectrum illustrates the presence of the singly (m/z ) and diphosphorylated (m/z ) peptides of AtPIP2;1 and/or AtPIP2;2 (see text) and of the singly (m/z ) and diphosphorylated (m/z ) peptides of AtPIP2;7. *, metastable decomposition of peptide with m/z a.i., absolute intensity. Sodana Prak et al. Mol Cell Proteomics 2008;7: © 2008 The American Society for Biochemistry and Molecular Biology

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Quantification of intracellular fuzzy staining (A) and of spherical bodies (B) in root cells upon an NaCl treatment. Quantification of intracellular fuzzy.

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Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. Role of C-terminal phosphorylation in the subcellular.

Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1 in response to salinity. Role of C-terminal phosphorylation in the subcellular.
Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.

Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.
Correlation of log-transformed signal intensity from two Affymetrix microarray hybridizations using platelet RNA. Plotted are those probesets with an average.

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Sequence alignment of C-terminal phosphorylated plant aquaporins

Sequence alignment of C-terminal phosphorylated plant aquaporins
Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.

Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z 1188.53).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).
Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence.

Role of C-terminal phosphorylation in the subcellular localization of AtPIP2;1.A, the figure shows typical laser-scanning confocal micrographs of the fluorescence.
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

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Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,

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Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
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Novel phosphorylation sites on H+-ATPase proteins

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