Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain.

FEBS Lett.2015 Oct 24;589(21):3237-41. Epub 2015 Oct 03

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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 (15)N-(1)H 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.

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Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain.

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