Effects of a Mechanical Stimulation on Localization of Annexin-Like Proteins in Bryonia dioica Internodes

Thonat, Catherine; Mathieu, Chantal; Crèvecœur, Michèle; Penel, Claude; Gaspar, Thomas; Boyer, Nicole

doi:10.1104/pp.114.3.981

Cited by 44 publications

(22 citation statements)

References 36 publications

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“…1). A prominent feature of plant-type annexins was the existence of (at least) two annexin proteins in every plant species investigated so far (29,(31)(32)(33); thus, a second annexin, Anx(Ca38), is found in C. annuum. The two proteins Anx24(Ca32) and Anx(Ca38) differ not only in their primary structure but also in their migration behavior on SDS-PAGE, despite having nearly the same molecular weights.…”

Section: Resultsmentioning

confidence: 99%

Annexin 24 from Capsicum annuum

Hofmann¹,

Proust²,

Dorowski³

et al. 2000

Journal of Biological Chemistry

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This work provides the first three-dimensional structure of a member of the plant annexin family and correlates these findings with biochemical properties of this protein. Annexin 24(Ca32) from Capsicum annuum was purified as a native protein from bell pepper and was also prepared by recombinant techniques. To overcome the problem of precipitation of the recombinant wildtype protein in crystallization trials, two mutants were designed. Whereas an N-terminal truncation mutant turned out to be an unstable protein, the N-terminal His-tagged annexin 24(Ca32) was crystallized, and the three-dimensional structure was determined by x-ray diffraction at 2.8 Å resolution. The structure refined to an R-factor of 0.216 adopts the typical annexin fold; the detailed structure, however, is different from non-plant annexins, especially in domains I and III and in the membrane binding loops on the convex side. Within the unit cell there are two molecules per asymmetric unit, which differ in conformation of the IAB-loop. Both conformers show Trp-35 on the surface. The loop-out conformation is stabilized by tight interactions of this tryptophan with residue side chains of a symmetry-related molecule and enforced by a bound sulfate. Characterization of this plant annexin using biophysical methods revealed calcium-dependent binding to phospholipid vesicles with preference for phosphatidylcholine over phosphatidylserine and magnesium-dependent phosphodiesterase activity in vitro as shown with adenosine triphosphate as the substrate. A comparative unfolding study of recombinant annexin 24(Ca32) wild type and of the His-tag fusion protein indicates higher stability of the latter. The effect of this N-terminal modification is also visible from CD spectra. Both proteins were subjected to a FURA-2-based calcium influx assay, which gave high influx rates for the wild-type but greatly reduced influx rates for the fusion protein. We therefore conclude that the N-terminal domain is indeed a major regulatory element modulating different annexin properties by allosteric mechanisms.Annexins have been a focus of research for nearly 20 years, and a large amount of data has accumulated especially for mammalian members of this protein family although annexin proteins are abundant throughout all species but yeast. In 1989, the first annexin-like proteins in plants were identified (1), and it is now well established that annexins are just as ubiquitous in the plant kingdom as elsewhere. The amount of annexin in plant cells makes up to 0.1% of the total protein content (2). As deduced from amino acid sequences, plant-type and vertebrate annexins show similarities up to 40%, whereas the plant-type members share up to 97% similarity with each other (see Table I). A more detailed analysis of the phylogenetic aspects led to the conclusion that within the overall annexin family a unique subset is made up by the plant-type members. In contrast to mammalian and vertebrate tissues, where varying amounts of different annexin proteins are expressed, plants poss...

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Section: Resultsmentioning

confidence: 99%

Annexin 24 from Capsicum annuum

Hofmann¹,

Proust²,

Dorowski³

et al. 2000

Journal of Biological Chemistry

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“…In most cases, plant annexin is localized to intracellular membranes or to the cytoplasm (Blackbourn et al 1992;Clark et al 1992Clark et al , 1994Clark and Roux 1995;Seals and Randall 1997;Thonat et al 1997), with the exception of alfalfa annexin, which is localized to the nucleus (Kova´cs et al 1998). Annexin from Bryonia dioica is detected throughout the cytoplasm in parenchymal cells from untreated internodes and accumulates near the plasma membrane 30 min after rubbing (Thonat et al 1997).…”

Section: Discussionmentioning

confidence: 98%

Biochemical and immunohistochemical characterization of Mimosa annexin

Hoshino

Hayashi

Temmei

et al. 2004

Planta

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To characterize the biochemical properties of plant annexin, we isolated annexin from Mimosa pudica L. and analyzed the biochemical properties conserved between Mimosa annexin and animal annexins, e.g. the ability to bind phospholipid and F-actin in the presence of calcium. We show that Mimosa annexin is distributed in a wide variety of tissues. Immunoblot analysis also revealed that the amount of annexin is developmentally regulated. To identify novel functions of Mimosa annexin, we examined the pattern of distribution and the regulation of its expression in the pulvinus. The amount of annexin in the pulvinus increased at night and was sensitive to abscisic acid; however, there was no detectable induction of annexin by cold or mechanical stimulus. Annexin distribution in the cell periphery during the daytime was changed to a cytoplasmic distribution at night, indicating that Mimosa annexin may contribute to the nyctinastic movement in the pulvinus.

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“…In its extracellular form, the channel-forming annexin ANXA5 regulates Polycystin-1 (a transient receptor potential channel) at its extracellular N terminus (Markoff et al, 2007), while extracellular ANXA1 causes [Ca 2+ ] cyt increase by activating plasma membrane G-protein-coupled receptors (Babbin et al, 2006). Generally, the known abundance of annexins in the cytosol and their ability to relocate to plasma and endomembranes (Thonat et al, 1997;Breton et al, 2000;Lee et al, 2004;reviewed in Mortimer et al, 2008) place them predominantly as intracellular regulators of [Ca 2+ ] cyt . In this respect, annexins, as regulators of plant channels, can be viewed as being similar to calmodulin.…”

Section: Discussionmentioning

confidence: 99%

“…Maize (Zea mays) annexins have been found to stimulate Ca 2+ -dependent exocytosis in root cap cells (Carroll et al, 1998), the process underlying cell expansion and plant growth (Carroll et al, 1998). Annexin relocation from the cytosol to membranes can occur in response to specific stimuli, such as touch (Thonat et al, 1997), cold (Breton et al, 2000), and salinity , suggesting a role in adaptive signaling. Indeed, Arabidopsis thaliana annexin 1 (ANN1) expression is upregulated by peroxide, salicylic acid (Gidrol et al, 1996), abscisic acid , drought, cold, and salt stress (Cantero et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Zea mays Annexins Modulate Cytosolic Free Ca2+ and Generate a Ca2+-Permeable Conductance

et al. 2009

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Regulation of reactive oxygen species and cytosolic free calcium ([Ca 2+ ] cyt ) is central to plant function. Annexins are small proteins capable of Ca 2+ -dependent membrane binding or membrane insertion. They possess structural motifs that could support both peroxidase activity and calcium transport. Here, a Zea mays annexin preparation caused increases in [Ca 2+ ] cyt when added to protoplasts of Arabidopsis thaliana roots expressing aequorin. The pharmacological profile was consistent with annexin activation (at the extracellular plasma membrane face) of Arabidopsis Ca 2+ -permeable nonselective cation channels. Secreted annexins could therefore modulate Ca 2+ influx. As maize annexins occur in the cytosol and plasma membrane, they were incorporated at the intracellular face of lipid bilayers designed to mimic the plasma membrane. Here, they generated an instantaneously activating Ca 2+ -permeable conductance at mildly acidic pH that was sensitive to verapamil and Gd 3+ and had a Ca 2+ -to-K + permeability ratio of 0.36. These results suggest that cytosolic annexins create a Ca 2+ influx pathway directly, particularly during stress responses involving acidosis. A maize annexin preparation also demonstrated in vitro peroxidase activity that appeared independent of heme association. In conclusion, this study has demonstrated that plant annexins create Ca 2+ -permeable transport pathways, regulate [Ca 2+ ] cyt , and may function as peroxidases in vitro.

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Effects of a Mechanical Stimulation on Localization of Annexin-Like Proteins in Bryonia dioica Internodes

Cited by 44 publications

References 36 publications

Annexin 24 from Capsicum annuum

Annexin 24 from Capsicum annuum

Biochemical and immunohistochemical characterization of Mimosa annexin

Zea mays Annexins Modulate Cytosolic Free Ca2+ and Generate a Ca2+-Permeable Conductance

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