Detection of Phytochrome Phosphorylation in Plants

Eva Klement, Péter Gyula, András Viczián

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Posttranslational modification (PTM) of proteins occurs during or after translation and in most cases means covalent binding of a functional group to certain amino acid side chains. Among PTMs, phosphorylation is extensively studied for decades. During phosphorylation, a phosphate group is added to the target residue that is dominantly serine, threonine, and tyrosine in eukaryotes. The phosphate group attachment is catalyzed by kinases, whereas the removal of phosphate (dephosphorylation) is performed by phosphatases. Phosphorylation of phytochrome photoreceptors alters light signaling in multiple ways, thus the examination of this PTM is an expanding aspect of light signaling research. Although this chapter presents methods for detecting phosphorylated phytochrome B molecules, it can be applied on other phytochrome species. The first presented protocol of this chapter shows how the phosphorylation state of phytochrome photoreceptors can be monitored in a modified polyacrylamide gel electrophoresis system. The second protocol describes in detail how phosphorylated amino acids of a target molecule can be identified using mass spectrometry analysis.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages41-67
Number of pages27
DOIs
Publication statusPublished - Jan 1 2019

Publication series

NameMethods in Molecular Biology
Volume2026
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

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Keywords

  • Immunoblot
  • Immunoprecipitation
  • Mass spectrometry
  • Phos-tag
  • Phosphate
  • Posttranslational modification

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Klement, E., Gyula, P., & Viczián, A. (2019). Detection of Phytochrome Phosphorylation in Plants. In Methods in Molecular Biology (pp. 41-67). (Methods in Molecular Biology; Vol. 2026). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-9612-4_4