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Record 1 of 1693
Technical advance: identification of plant actin-binding proteins by F-actin affinity chromatography
External Online Source: doi:10.1046/j.1365-313x.2000.00852.x
Author and Affiliation:
Hu, S.(Wake Forest University, Department of Biology, Winston-Salem, NC 27109, United States)
Brady, S. R.
Kovar, D. R.
Staiger, C. J.
Clark, G. B.
Roux, S. J.
Muday, G. K.
Abstract: Proteins that interact with the actin cytoskeleton often modulate the dynamics or organization of the cytoskeleton or use the cytoskeleton to control their localization. In plants, very few actin-binding proteins have been identified and most are thought to modulate cytoskeleton function. To identify actin-binding proteins that are unique to plants, the development of new biochemical procedures will be critical. Affinity columns using actin monomers (globular actin, G-actin) or actin filaments (filamentous actin, F-actin) have been used to identify actin-binding proteins from a wide variety of organisms. Monomeric actin from zucchini (Cucurbita pepo L.) hypocotyl tissue was purified to electrophoretic homogeneity and shown to be native and competent for polymerization to actin filaments. G-actin, F-actin and bovine serum albumin affinity columns were prepared and used to separate samples enriched in either soluble or membrane-associated actin-binding proteins. Extracts of soluble actin-binding proteins yield distinct patterns when eluted from the G-actin and F-actin columns, respectively, leading to the identification of a putative F-actin-binding protein of approximately 40 kDa. When plasma membrane-associated proteins were applied to these columns, two abundant polypeptides eluted selectively from the F-actin column and cross-reacted with antiserum against pea annexins. Additionally, a protein that binds auxin transport inhibitors, the naphthylphthalamic acid binding protein, which has been previously suggested to associate with the actin cytoskeleton, was eluted in a single peak from the F-actin column. These experiments provide a new approach that may help to identify novel actin-binding proteins from plants.
Publication Date: Oct 01, 2000
Document ID:
20040112721
(Acquired Oct 05, 2004)
Subject Category: LIFE SCIENCES (GENERAL)
Document Type: Journal Article
Publication Information: The Plant journal : for cell and molecular biology (ISSN 0960-7412); Volume 24; 1; 127-37
Publisher Information: United Kingdom
Description: In English
Distribution Limits: Unclassified; Publicly available; Unlimited
Rights: Copyright
NASA Terms: CHROMATOGRAPHY; MUSCLE FIBERS; PLANTS (BOTANY); PROTEINS; VEGETABLES; CELL MEMBRANES (BIOLOGY); CORN; ELECTROPHORESIS; HISTOCHEMICAL ANALYSIS; IMMUNOLOGY; LIQUID CHROMATOGRAPHY; STEMS
Other Descriptors: ACTINS/METABOLISM; MICROFILAMENT PROTEINS/ISOLATION & PURIFICATION/METABOLISM; PLANT PROTEINS/ISOLATION & PURIFICATION/METABOLISM; VEGETABLES/CHEMISTRY/METABOLISM; CELL MEMBRANE/CHEMISTRY; CHROMATOGRAPHY, AFFINITY/METHODS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYPOCOTYL/CHEMISTRY; IMMUNOBLOTTING; SUPPORT, U.S. GOV'T, NON-P.H.S; ZEA MAYS/METABOLISM; NASA DISCIPLINE PLANT BIOLOGY; NON-NASA CENTER
Availability Source: Other Sources
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