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Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain
- O’Connell, Nichole E., Lelli, Katherine, Mann, Richard S., Palmer, Arthur G.
- FEBS letters 2015 v.589 no.21 pp. 3237-3241
- DNA, Drosophila melanogaster, asparagine, deamidation, gel electrophoresis, nuclear magnetic resonance spectroscopy, post-translational modification, time series analysis, transcription factors
- Spontaneous deamidation of asparagine is a non-enzymatic post-translational modification of proteins. Residue Asn 321 is the main site of deamidation of the Drosophila melanogaster Hox transcription factor Sex Combs Reduced (Scr). Formation of iso-aspartate, the major deamidation product, is detected by HNCACB triple-resonance NMR spectroscopy. The rate of deamidation is quantified by fitting the decay of Asn NH2 side-chain signals in a time-series of 15N-1H HSQC NMR spectra. The deamidated form of Scr binds to specific DNA target sequences with reduced affinity as determined by an electrophoretic mobility shift assay.