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Characterization of residue‐dependent differences in the peripheral membrane association of the FATC domain of the kinase ‘target of rapamycin’ by NMR and CD spectroscopy
Author(s) -
Sommer Lisa A.M.,
Dames Sonja A.
Publication year - 2014
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 - 10.1016/j.febslet.2014.03.031
Subject(s) - model lipid bilayer , nuclear magnetic resonance spectroscopy , micelle , mutant , residue (chemistry) , vesicle , chemistry , membrane , protein kinase domain , biophysics , biochemistry , liposome , kinase , microbiology and biotechnology , biology , lipid bilayer , stereochemistry , aqueous solution , gene , lipid bilayer phase behavior
The conserved C‐terminal FATC domain of the kinase ‘target of rapamycin’ is important for its regulation and was suggested to contain a peripheral membrane anchor. Here, we present the characterization of the interactions of the yeast TOR1 FATC domain (2438–2470 = y1fatc) and 15 mutants with membrane mimetic micelles, bicelles, and small unilamellar vesicles (SUVs) by NMR and CD spectroscopy. Replacement of up to 6–7 residues did not result in a significant abrogation of the association with micelles or bicelles. However, replacement of only one residue could result in an impairment of the interaction with SUVs that are usually used at low concentrations. Some mutants not binding liposomes may be introduced in full‐length TOR for future functional and localization studies in vivo .