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Enhanced PKMT-substrate recognition through non active-site interactions.

Margarita Kublanovsky1, Amir Aharoni2, Dan Levy1

  • 1The Shraga Segal Department of Microbiology, Immunology and Genetics, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel; The National Institute for Biotechnology in the Negev (NIBN), Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.

Biochemical and Biophysical Research Communications
|May 21, 2018
PubMed
Summary
This summary is machine-generated.

Protein lysine methyltransferases (PKMTs) recognize globular substrates via interactions outside the active site, enhancing catalytic efficiency. SETD6 and SETD7 show higher affinity for full-length RelA protein than peptides.

Keywords:
Lysine methylationMolecular recognitionProtein lysine methyl-transferasesSETD6SETD7

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Protein lysine methyltransferases (PKMTs) modify proteins by methylating lysine residues.
  • Current understanding of PKMTs primarily focuses on active site-peptide interactions.
  • Recognition mechanisms for globular protein substrates remain largely unknown.

Purpose of the Study:

  • To investigate if PKMTs recognize substrates through interactions outside the active site.
  • To compare the activity of SETD6 and SETD7 with both peptide and full-length RelA substrates.
  • To elucidate the role of extra-active site interactions in PKMT substrate recognition.

Main Methods:

  • Utilized the MTase-Glo™ methyltransferase assay to measure enzyme activity.
  • Assessed activity using both peptide and full-length RelA substrates.
  • Calculated Michaelis-Menten (MM) parameters (KM) to determine interaction affinities.

Main Results:

  • PKMTs exhibited significantly higher affinity (up to ~12-fold lower KM) for full-length RelA protein compared to RelA peptides.
  • SETD6 and SETD7 demonstrated similar substrate recognition patterns for RelA.
  • Extra-active site interactions enhance PKMT catalytic efficiency and specificity for globular substrates.

Conclusions:

  • PKMTs, including SETD6 and SETD7, utilize interactions beyond the active site for substrate recognition.
  • These extra-active site interactions are crucial for enhancing catalytic efficiency and specificity.
  • Substrate recognition by PKMTs involves complex docking mechanisms for optimal cellular function.