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© Research
Publication : FEBS letters

Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 28 Sep 2016

Deville C, Girard-Blanc C, Assrir N, Nhiri N, Jacquet E, Bontems F, Renault L, Petres S, van Heijenoort C

Link to Pubmed [PMID] – 27680677

FEBS Lett. 2016 Sep;

Understanding the structural basis of actin cytoskeleton remodelling requires stabilization of actin monomers, oligomers and filaments in complex with partner proteins using various biochemical strategies. Here we report a dramatic destabilisation of the dynamic interaction with a model β-thymosin/WH2 domain induced by mutations in actin. This result underlines that mutant actins should be used with prudence to characterise interactions with intrinsically disordered partners as destabilisation of dynamic interactions, although identifiable by NMR, may be invisible to other structural techniques. It also highlights how both β -thymosin/WH2 domains and actin tune local structure and dynamics in regulatory processes involving intrinsically disordered domains. This article is protected by copyright. All rights reserved.

http://www.ncbi.nlm.nih.gov/pubmed/27680677