Bioorganic & medicinal chemistry, 2011-04, Vol.19 (7), p.2373-2377
2011
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Details
- Autor(en) / Beteiligte
- Titel
- Methylation-mediated control of aurora kinase B and Haspin with epigenetically modified histone H3 N-terminal peptides
- Ist Teil von
- Bioorganic & medicinal chemistry, 2011-04, Vol.19 (7), p.2373-2377
- Ort / Verlag
- Amsterdam: Elsevier Ltd
- Erscheinungsjahr
- 2011
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- If multiple post-translational modifications are responsible for important biological markers, additional specificity must be present to serve as embedded combinatorial markers for phosphorylation. In this investigation, we have attempted to elucidate the specificity of AURKB and Haspin by using peptides of various lengths that contain all possible methylations, acetylations, and phosphorylations in histone H3 N-terminal peptides. The activity of AURKB is affected by a wide range of modifications from R2 to K14, while that of Haspin is affected significantly by modifications at R2 and K4. In cases where kinase activity is reduced substantially by other modifications, dimethylation at R2 and R8 totally abolishes phosphorylation at S10 promoted by AURKB and as does dimethylation at R2 on Haspin promoted phosphorylation at T3.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0968-0896eISSN: 1464-3391DOI: 10.1016/j.bmc.2011.02.011Titel-ID: cdi_proquest_miscellaneous_862785802
- Format
- –
- Schlagworte
- Acetylation, Amino Acid Sequence, Analytical, structural and metabolic biochemistry, Aurora kinase, Aurora Kinase B, Aurora Kinases, Biological and medical sciences, biomarkers, Enzymes and enzyme inhibitors, Epigenomics, Fundamental and applied biological sciences. Psychology, Haspin, Histone H3, Histone H3 N-terminal peptide, histones, Histones - genetics, Histones - metabolism, Humans, Intracellular Signaling Peptides and Proteins - genetics, Intracellular Signaling Peptides and Proteins - metabolism, Medical sciences, Methylation, Methylation-mediated phosphorylation, Miscellaneous, Modification, Molecular Sequence Data, Peptide Fragments - genetics, Peptide Fragments - metabolism, peptides, Pharmacology. Drug treatments, Phosphorylation, Post-translation, post-translational modification, Protein Processing, Post-Translational, Protein-Serine-Threonine Kinases - genetics, Protein-Serine-Threonine Kinases - metabolism, Structure-Activity Relationship, Substrate Specificity, Transferases