On the Extent of Tyrosine Phosphorylation in Chloroplasts

Qintao Lu; Stefan Helm; Anja Rödiger; Sacha Baginsky

doi:10.1104/pp.15.00921

On the Extent of Tyrosine Phosphorylation in Chloroplasts

Plant Physiol. 2015 Oct;169(2):996-1000. doi: 10.1104/pp.15.00921. Epub 2015 Aug 4.

Authors

Qintao Lu¹, Stefan Helm¹, Anja Rödiger¹, Sacha Baginsky²

Affiliations

¹ Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (Q.L.); andInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, 06120 Halle (Saale), Germany (S.H., A.R., S.B.).
² Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (Q.L.); andInstitute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, 06120 Halle (Saale), Germany (S.H., A.R., S.B.) sacha.baginsky@biochemtech.uni-halle.de.

Abstract

Reanalysis of published mass spectrometry data on Tyr-phosphorylated chloroplast proteins indicates that the majority of peptide spectrum matches reporting Tyr phosphorylation are ambiguous.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Chloroplasts / metabolism*
Molecular Sequence Data
Phosphoproteins / analysis
Phosphoproteins / metabolism
Phosphorylation
Plant Proteins / analysis*
Plant Proteins / immunology
Plant Proteins / metabolism*
Proteomics / methods*
Software
Tyrosine / metabolism*

Substances

Phosphoproteins
Plant Proteins
Tyrosine