Actin-binding specificity of marine macrolide toxins, mycalolide B and kabiramide D.

Abstract:

:An actin-depolymerizing marine natural product, mycalolide B, and a related compound, kabiramide D, were labeled with biocytin, a biotin derivative, and used to specify target molecules in cultured rat 3Y1 fibroblasts. Mycalolide B exhibited the ability to bind to various intracellular proteins, probably through the Michael addition of a sulfhydryl group to C5 of mycalolide B. However, no intracellular proteins other than actin apparently reacted with biocytinylated kabiramide D, demonstrating that the binding of kabiramide D to actin was highly specific. Cells treated with biocytinylated kabiramide D followed by staining with fluorescein isothiocyanate-conjugated avidin showed that biocytinylated kabiramide D bound to stress fibers composed of F-actin, although the staining intensity was weaker than the fluorescent phalloidin staining. The assay for the binding of kabiramide D to actin, which had previously been treated with other actin-depolymerizing agents, showed that the actin-binding site for kabiramide D was the same as that for bistheonellide A, but not those for latrunculin A and cytochalasin D.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Wada S,Matsunaga S,Saito S,Fusetani N,Watabe S

doi

10.1093/oxfordjournals.jbchem.a022029

subject

Has Abstract

pub_date

1998-05-01 00:00:00

pages

946-52

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

123

pub_type

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