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Sommer, L.A.* ; Dames, S.A.

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.

FEBS Lett. 588, 1755-1766 (2014)
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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.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Bicelle ; Cd ; Kinase ; Liposome ; Membrane Mimetic ; Micelle ; Nmr ; Protein Lipid Interactions ; Protein Membrane Interactions ; Suv ; Target Of Rapamycin; Mammalian Target; Endoplasmic-reticulum; Binding Domain; Saccharomyces-cerevisiae; 3-dimensional Structure; Phosphatidic-acid; Growth-control; Lipid-binding; Localization; Complex
ISSN (print) / ISBN 0014-5793
e-ISSN 1873-3468
Journal FEBS Letters
Quellenangaben Volume: 588, Issue: 9, Pages: 1755-1766 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place Amsterdam
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)