Functional characterization of Val60, a key residue involved in the membrane‐oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea. Issue 15 (19th June 2015)

• Record Type: Journal Article
• Authors: Morante, Koldo; Caaveiro, Jose M.M.; Viguera, Ana Rosa; Tsumoto, Kouhei; González-Mañas, Juan Manuel
• Is Part Of: FEBS letters. Volume 589:Issue 15(2015)
• Page Start: 1840
• Page End: 1846
• Publication Date: 2015-06-19
• Subjects: PFT -- pore-forming toxins -- FraC -- fragaceatoxin C -- RBC -- red blood cells -- SM -- sphingomyelin -- PC -- chicken egg l-α-phosphatidylcholine -- LUV -- large unilamellar vesicle -- SEC -- size-exclusion chromatography -- DDM -- n-dodecyl β-d-maltopyranoside -- HC50 -- protein concentration required for 50% lysis -- TM -- denaturation temperature -- CD -- circular dichroism -- Pore-forming toxins -- Protein oligomerization -- Lipid–protein interaction -- Model membranes; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.06.012
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : To gain insight into the mechanism of toxin oligomerization, different point mutations have been introduced at this position. Functional characterization of the muteins suggests that Val60 represents a hot‐spot where the introduction of mutations hinders protein assembly and reduces the overall affinity for membranes. Abstract : Valine 60 is a crucial residue involved in oligomerization of actinoporins. Mutations at this position interfere with oligomerization and reduce the overall affinity for membranes. Actinoporin oligomerization is an enthalpy‐driven process.