Literature DB >> 26435141

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

Nichole E O'Connell1, Katherine Lelli1, Richard S Mann1, Arthur G Palmer2.   

Abstract

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.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Asparagine deamidation; DNA binding; Dissociation constant; Hox transcription factor; NMR spectroscopy; Sex Combs Reduced

Mesh:

Substances:

Year:  2015        PMID: 26435141      PMCID: PMC4674082          DOI: 10.1016/j.febslet.2015.09.020

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  19 in total

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2.  Post-translational modifications of Drosophila melanogaster HOX protein, Sex combs reduced.

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  2 in total

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