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Control of protein phosphorylation with a genetically encoded photocaged amino acid

Academic Article
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Overview

authors

  • Lemke, E. A.
  • Summerer, D.
  • Geierstanger, B. H.
  • Brittain, S. M.
  • Schultz, Peter

publication date

  • December 2007

journal

  • Nature Chemical Biology  Journal

abstract

  • We genetically encoded the photocaged amino acid 4,5-dimethoxy-2-nitrobenzylserine (DMNB-Ser) in Saccharomyces cerevisiae in response to the amber nonsense codon TAG. This amino acid was converted to serine in living cells by irradiation with relatively low-energy blue light and was used to noninvasively photoactivate phosphorylation of the transcription factor Pho4, which controls the cellular response to inorganic phosphate. When substituted at phosphoserine sites that control nuclear export of Pho4, blocks phosphorylation and subsequent export by the receptor Msn5 (ref. 2). We triggered phosphorylation of individual serine residues with a visible laser pulse and monitored nuclear export of Pho4-GFP fusion constructs in real time. We observed distinct export kinetics for differentially phosphorylated Pho4 mutants, which demonstrates dynamic regulation of Pho4 function. This methodology should also facilitate the analysis of other cellular processes involving free serine residues, including catalysis, biomolecular recognition and ion transport.

subject areas

  • DNA-Binding Proteins
  • Molecular Structure
  • Mutation
  • Nitrobenzenes
  • Phosphorylation
  • Photochemistry
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Serine
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.2007.44

PubMed ID

  • 17965709
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Additional Document Info

start page

  • 769

end page

  • 772

volume

  • 3

issue

  • 12

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