Isolation of an abundant 50,000-dalton actin filament bundling protein from dictyostelium amoebae

Mark Demma, Vivien Warren, Rick Hock, Suranganie Dharmawardhane, John S. Condeelis

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Abstract

A monomeric actin bundling protein with a native molecular weight of approximately 50,000 (ABP-50) has been isolated from amoebae of Dictyostelium discoideum. ABP-50 cross-links F-actin to form tightly packed bundles, some of which are highly ordered. It exhibits a Kd of 2.1 μM and a molar ratio to actin of 1:1 in bundles. Calcium and ATP at physiological concentrations have no effect on these activities. ABP-50 is immunologically unrelated to 30-kDa protein, a previously described bundling protein from Dictyostelium. Immunofluorescence with affinity-purified polyclonal antibodies indicates that ABP-50 is localized in regions of the amoeboid cell cortex containing actin bundles. The molar ratio of ABP-50 to actin is approximately 1:5 in vivo. Therefore, the abundance of ABP-50 suggests that it may be responsible for the majority of the bundling activity in these cells.

Original languageEnglish (US)
Pages (from-to)2286-2291
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number4
StatePublished - Feb 5 1990

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Amoeba
Dictyostelium
Actins
Proteins
Fluorescent Antibody Technique
Adenosine Triphosphate
Molecular Weight
Molecular weight
actin filament bundling proteins
Calcium
Antibodies

ASJC Scopus subject areas

  • Biochemistry

Cite this

Isolation of an abundant 50,000-dalton actin filament bundling protein from dictyostelium amoebae. / Demma, Mark; Warren, Vivien; Hock, Rick; Dharmawardhane, Suranganie; Condeelis, John S.

In: Journal of Biological Chemistry, Vol. 265, No. 4, 05.02.1990, p. 2286-2291.

Research output: Contribution to journalArticle

Demma, Mark ; Warren, Vivien ; Hock, Rick ; Dharmawardhane, Suranganie ; Condeelis, John S. / Isolation of an abundant 50,000-dalton actin filament bundling protein from dictyostelium amoebae. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 4. pp. 2286-2291.
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