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

Understanding the structural basis of actin cytoskeleton remodeling requires stabilization of actin monomers, oligomers, and filaments in complex with partner proteins, using various biochemical strategies. Here, we report a dramatic destabilization of the dynamic interaction with a model β‐thymosin...

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Bibliographic Details
Published in:FEBS letters 2016-10, Vol.590 (20), p.3690-3699
Main Authors: Deville, Célia, Girard‐Blanc, Christine, Assrir, Nadine, Nhiri, Naïma, Jacquet, Eric, Bontems, François, Renault, Louis, Petres, Stéphane, Heijenoort, Carine
Format: Article
Language:English
Subjects:
actin
Actins - chemistry
Actins - genetics
Animals
Crystallography, X-Ray
dynamic interaction
Life Sciences
Models, Molecular
Mutation
NMR spectroscopy
Protein Binding
Protein Conformation
Rabbits
Sequence Homology, Amino Acid
Thymosin - chemistry
β‐thymosin/WH2 domains
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Summary:Understanding the structural basis of actin cytoskeleton remodeling requires stabilization of actin monomers, oligomers, and filaments in complex with partner proteins, using various biochemical strategies. Here, we report a dramatic destabilization 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 characterize interactions with intrinsically disordered partners as destabilization 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.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12423