|
THE PLANT CELL, Vol 8, Issue 2 333-342, Copyright © 1996 by American Society of Plant Biologists
Tomato Annexins p34 and p35 Bind to F-Actin and Display Nucleotide Phosphodiesterase Activity Inhibited by Phospholipid Binding
C. M. Calvert, S. J. Gant and D. J. Bowles
The Plant Laboratory, Department of Biology, University of York, P.O. Box 373, York YO1 5YW, United Kingdom
Annexins are a family of proteins found in a range of eukaryotic cell
types. They share a characteristic amino acid sequence and a Ca2+-dependent
affinity for specific phospholipids. In plants, proteins with common
properties and significant homology with annexins have been identified in a
number of species and implicated in diverse cellular functions known to be
modulated by Ca2+. This study describes several novel biochemical
properties of the tomato annexins p34 and p35 that are relevant to our
understanding of their functions in the plant. First, the annexins were
found to bind to actin in a calcium- and pH-dependent interaction that was
specific for F-actin and not G-actin. Second, an enzyme activity defined as
a nucleotide phosphodiesterase activity was found associated with the
purified annexin preparation. Selective immunoprecipitation of p34 and p35
strongly suggests that the enzyme activity is a property of the annexins
and constitutes 60% of the total soluble activity found in root extracts
capable of hydrolyzing free ATP. The substrate specificity of the enzyme
within in vitro assays is broad. ATP is the preferred substrate, but nearly
identical rates of hydrolysis of GTP and substantial hydrolysis of other
nucleotide tri- and diphosphates are observed. The enzyme activity was
found to be a property of both p34 and p35, although the specific activity
was routinely higher for p34. Third, the enzyme activity of the annexins
was not affected by F-actin binding but could be abolished by the specific
Ca2+-dependent interaction of the annexins with phospholipids. Our results
showed that p34 and p35 account for substantial enzyme activity in tomato
root cells. This activity was exhibited when the proteins were either in
soluble form or attached to actin filaments. Enzyme activity was not
exhibited when the annexins were bound to phospholipids. These properties
suggest a role for the proteins in mediating Ca2+-dependent events
involving interactions of the cytoskeleton and cellular membranes.
This article has been cited by other articles:
|
|
|
|
 
J. C. Mortimer, A. Laohavisit, N. Macpherson, A. Webb, C. Brownlee, N. H. Battey, and J. M. Davies
Annexins: multifunctional components of growth and adaptation
J. Exp. Bot.,
February 10, 2008;
(2008)
erm344v1.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. M. Gorecka, C. Thouverey, R. Buchet, and S. Pikula
Potential Role of Annexin AnnAt1 from Arabidopsis thaliana in pH-Mediated Cellular Response to Environmental Stimuli
Plant Cell Physiol.,
June 1, 2007;
48(6):
792 - 803.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. J. Bushart and S. J. Roux
Conserved Features of Germination and Polarized Cell Growth: A Few Insights from a Pollen-Fern Spore Comparison
Ann. Bot.,
January 1, 2007;
99(1):
9 - 17.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Lee, E. J. Lee, E. J. Yang, J. E. Lee, A. R. Park, W. H. Song, and O. K. Park
Proteomic Identification of Annexins, Calcium-Dependent Membrane Binding Proteins That Mediate Osmotic Stress and Abscisic Acid Signal Transduction in Arabidopsis
PLANT CELL,
June 1, 2004;
16(6):
1378 - 1391.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
G. B. Clark, A. Sessions, D. J. Eastburn, and S. J. Roux
Differential Expression of Members of the Annexin Multigene Family in Arabidopsis
Plant Physiology,
July 1, 2001;
126(3):
1072 - 1084.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
G. Schwarz, J. Schulze, F. Bittner, T. Eilers, J. Kuper, G. Bollmann, A. Nerlich, H. Brinkmann, and R. R. Mendel
The Molybdenum Cofactor Biosynthetic Protein Cnx1 Complements Molybdate-Repairable Mutants, Transfers Molybdenum to the Metal Binding Pterin, and Is Associated with the Cytoskeleton
PLANT CELL,
December 1, 2000;
12(12):
2455 - 2472.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
K. Yuasa and M. Maeshima
Purification, Properties, and Molecular Cloning of a Novel Ca2+-Binding Protein in Radish Vacuoles
Plant Physiology,
November 1, 2000;
124(3):
1069 - 1078.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
A. Hofmann, J. Proust, A. Dorowski, R. Schantz, and R. Huber
Annexin 24 from Capsicum annuum. X-RAY STRUCTURE AND BIOCHEMICAL CHARACTERIZATION
J. Biol. Chem.,
March 10, 2000;
275(11):
8072 - 8082.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H. Shin and R. M. Brown Jr.
GTPase Activity and Biochemical Characterization of a Recombinant Cotton Fiber Annexin
Plant Physiology,
March 1, 1999;
119(3):
925 - 934.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
E.-K. Lim, M. R. Roberts, and D. J. Bowles
Biochemical Characterization of Tomato Annexin p35. INDEPENDENCE OF CALCIUM BINDING AND PHOSPHATASE ACTIVITIES
J. Biol. Chem.,
December 25, 1998;
273(52):
34920 - 34925.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. A. Collings, T. Asada, N. S. Allen, and H. Shibaoka
Plasma Membrane-Associated Actin in Bright Yellow 2 Tobacco Cells . Evidence for Interaction with Microtubules
Plant Physiology,
November 1, 1998;
118(3):
917 - 928.
[Abstract]
[Full Text]
|
|
|
|
|
