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A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity.

Publication ,  Journal Article
Burg, JM; Makhoul, AT; Pemble, CW; Link, JE; Heller, FJ; McCafferty, DG
Published in: FEBS letters
August 2015

A target with therapeutic potential, lysine-specific demethylase 1A (KDM1A) is a regulator of gene expression whose tower domain is a protein-protein interaction motif. This domain facilitates the interaction of KDM1A with coregulators and multiprotein complexes that direct its activity to nucleosomes. We describe the design and characterization of a chimeric 'towerless' KDM1A, termed nΔ150 KDM1AΔTower KDM1B chimera (chKDM1AΔTower), which incorporates a region from the paralog lysine-specific demethylase 1B (KDM1B). This chimera copurifies with FAD and displays demethylase activity, but fails to bind the partner protein corepressor of the RE1-silencing transcription factor (CoREST). We conclude that KDM1A catalysis can be decoupled from tower-dependent interactions, lending chKDM1AΔTower useful for dissecting molecular contributions to KDM1A function.

Duke Scholars

Published In

FEBS letters

DOI

EISSN

1873-3468

ISSN

0014-5793

Publication Date

August 2015

Volume

589

Issue

18

Start / End Page

2340 / 2346

Related Subject Headings

  • Sequence Deletion
  • Recombinant Fusion Proteins
  • Protein Structure, Tertiary
  • Protein Engineering
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • Histone Demethylases
  • Biochemistry & Molecular Biology
  • Amino Acid Sequence
 

Citation

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ICMJE
MLA
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Burg, J. M., Makhoul, A. T., Pemble, C. W., Link, J. E., Heller, F. J., & McCafferty, D. G. (2015). A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity. FEBS Letters, 589(18), 2340–2346. https://doi.org/10.1016/j.febslet.2015.07.028
Burg, Jonathan M., Alan T. Makhoul, Charles W. Pemble, Jennifer E. Link, Frederick J. Heller, and Dewey G. McCafferty. “A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity.FEBS Letters 589, no. 18 (August 2015): 2340–46. https://doi.org/10.1016/j.febslet.2015.07.028.
Burg JM, Makhoul AT, Pemble CW, Link JE, Heller FJ, McCafferty DG. A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity. FEBS letters. 2015 Aug;589(18):2340–6.
Burg, Jonathan M., et al. “A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity.FEBS Letters, vol. 589, no. 18, Aug. 2015, pp. 2340–46. Epmc, doi:10.1016/j.febslet.2015.07.028.
Burg JM, Makhoul AT, Pemble CW, Link JE, Heller FJ, McCafferty DG. A rationally-designed chimeric KDM1A/KDM1B histone demethylase tower domain deletion mutant retaining enzymatic activity. FEBS letters. 2015 Aug;589(18):2340–2346.
Journal cover image

Published In

FEBS letters

DOI

EISSN

1873-3468

ISSN

0014-5793

Publication Date

August 2015

Volume

589

Issue

18

Start / End Page

2340 / 2346

Related Subject Headings

  • Sequence Deletion
  • Recombinant Fusion Proteins
  • Protein Structure, Tertiary
  • Protein Engineering
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • Histone Demethylases
  • Biochemistry & Molecular Biology
  • Amino Acid Sequence