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Engineered bromodomains to explore the acetylproteome.

Bryan D Bryson1, Amanda M Del Rosario, Jonathan S Gootenberg

  • 1Department of Biological Engineering, MIT, Cambridge, MA, USA; David H. Koch Institute for Integrative Cancer Research, MIT, Cambridge, MA, USA.

Proteomics
|February 3, 2015
PubMed
Summary
This summary is machine-generated.

Bromodomains, proteins that recognize acetylation, show diverse specificities. Engineered bromodomain pairs improve enrichment of acetylated peptides for mass spectrometry analysis.

Keywords:
Affinity reagentBromodomainLysine acetylationPosttranslational modificationProtein engineeringTechnology

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Acetylation regulates key biological processes like gene regulation and metabolism.
  • Current anti-acetyllysine antibodies for enrichment have limitations, including high nonspecific binding and lot variability.

Purpose of the Study:

  • To evaluate bromodomains as alternative affinity reagents for acetylated peptide enrichment.
  • To develop improved bromodomain-based enrichment strategies for mass spectrometry (MS).

Main Methods:

  • Generation of all known yeast bromodomain recombinant proteins.
  • Determination of bromodomain specificity using degenerate peptide arrays.
  • Enrichment of acetylated peptides from complex mixtures using selected bromodomains and MS analysis.
  • Engineering of combinatorial tandem bromodomain pairs to enhance affinity and utility.

Main Results:

  • Bromodomains exhibit a wide range of specificities for acetylated peptides.
  • Selected bromodomains successfully enriched acetylated peptides from complex biological samples.
  • Engineered tandem bromodomain pairs demonstrated improved utility for MS-based acetylproteomics.

Conclusions:

  • Bromodomains are viable alternatives to antibodies for acetylated peptide enrichment.
  • Engineered bromodomain affinity reagents offer enhanced capabilities for MS-based acetylproteomics.