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Mutations in actin used for structural studies partially disrupt β‐thymosin/WH2 domains interaction
Author(s) -
Deville Célia,
GirardBlanc Christine,
Assrir Nadine,
Nhiri Naïma,
Jacquet Eric,
Bontems François,
Renault Louis,
Petres Stéphane,
Heijenoort Carine
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12423
Subject(s) - actin , actin remodeling , cytoskeleton , biophysics , microbiology and biotechnology , thymosin , actin cytoskeleton , mutant , domain (mathematical analysis) , chemistry , biology , cell , biochemistry , gene , mathematical analysis , mathematics
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.