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Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC

We used bacterially expressed beta-galactosidase fusion proteins to localize the phospholipid binding domain of Acanthamoeba myosin IC to the region between amino acids 701 and 888 in the NH2-terminal half of the tail. Using a novel immobilized ligand lipid binding assay, we determined that myosin I...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289509/
https://www.ncbi.nlm.nih.gov/pubmed/1607386
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description We used bacterially expressed beta-galactosidase fusion proteins to localize the phospholipid binding domain of Acanthamoeba myosin IC to the region between amino acids 701 and 888 in the NH2-terminal half of the tail. Using a novel immobilized ligand lipid binding assay, we determined that myosin I can bind to several different acidic phospholipids, and that binding requires a minimum of 5 mol% acidic phospholipid in a neutral lipid background. The presence of di- and triglycerides and sterols in the lipid bilayer do not contribute to the affinity of myosin I for membranes. We confirm that the ATP-insensitive actin binding site is contained in the COOH-terminal 30 kD of the tail as previously shown for Acanthamoeba myosin IA. We conclude that the association of the myosin IC tail with acidic phospholipid head groups supplies much of the energy for binding myosin I to biological membranes, but probably not specificity for targeting myosin I isoforms to different cellular locations.
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spelling pubmed-22895092008-05-01 Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC J Cell Biol Articles We used bacterially expressed beta-galactosidase fusion proteins to localize the phospholipid binding domain of Acanthamoeba myosin IC to the region between amino acids 701 and 888 in the NH2-terminal half of the tail. Using a novel immobilized ligand lipid binding assay, we determined that myosin I can bind to several different acidic phospholipids, and that binding requires a minimum of 5 mol% acidic phospholipid in a neutral lipid background. The presence of di- and triglycerides and sterols in the lipid bilayer do not contribute to the affinity of myosin I for membranes. We confirm that the ATP-insensitive actin binding site is contained in the COOH-terminal 30 kD of the tail as previously shown for Acanthamoeba myosin IA. We conclude that the association of the myosin IC tail with acidic phospholipid head groups supplies much of the energy for binding myosin I to biological membranes, but probably not specificity for targeting myosin I isoforms to different cellular locations. The Rockefeller University Press 1992-06-02 /pmc/articles/PMC2289509/ /pubmed/1607386 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title_full Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title_fullStr Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title_full_unstemmed Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title_short Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
title_sort localization and specificity of the phospholipid and actin binding sites on the tail of acanthamoeba myosin ic
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289509/
https://www.ncbi.nlm.nih.gov/pubmed/1607386