Abstract
Monomeric actin (G-actin) is a small (42,000 Da) globular protein that polymerizes into higher order structures called microfilaments or filamentous actin (F- actin) (for a detailed review see [36]). These cytoskeletal polymers form a dynamic filament network in plant cells and support many fundamental processes, including cytoplasmic streaming, organelle positioning, cytokinesis, wound repair, responses to pathogen-attack, and cellular morphogenesis (for reviews see [23, 25, 26, 38]). Angiosperms contain large multigene families for actin and actin binding proteins (ABPs), and the biochemical and cell biological characterization of these components have received considerable attention in the past several years. A wealth of data is available for the motor molecule myosin and the small ABPs, profilin, and actin depolymerizing factor (reviewed in [3, 23, 26, 37]).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Andersland JM, Jagendorf AT and Parthasarathy MV (1992) The isolation of actin from pea roots by DNase I affinity chromatography. Plant Physiol 100: 1716–1723.
Andersland JM and Parthasarathy MV (1993) Conditions affecting depolymerization of actin in plant homogenates. J Cell Sci 104: 1273–1279.
Asada T and Collings D (1997) Molecular motors in higher plants. Trends Plant Sci 2: 29–37.
Carlier M-F, Laurent V, Santolini J, Melki R, Didry D, Xia G-X, Hong Y, Chua N-H and Pantaloni D (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility. J Cell Biol 136: 1307–1322.
Clarke SR, Staiger CJ, Gibbon BC and Franklin-Tong VE (1998) A potential signaling role for profilin in pollen of Papaver rhoeas. Plant Cell 10: 967–979.
Cooper JA and Pollard TD (1982) Methods to measure actin polymerization. Methods Enzymol 85: 182–210.
Fedorov AA, Pollard TD and Almo SC (1994) Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli. J Mol Biol 241: 480–482.
Ghosh G and Biswas S (1988) An actin of higher plant: Purification and characterization. Pl Physiol Biochem 15: 153–160.
Gibbon BC, Ren H and Staiger CJ (1997) Characterization of maize (Zea mays) pollen profilin function in vitro and in live cells. Biochem J 327: 909–915.
Gibbon BC, Zonia LE, Kovar DR, Hussey PJ and Staiger CJ (1998) Pollen profilin function depends on interaction with proline-rich motifs. Plant Cell 10: 981–993. [A printed Correction appeared in Aug. (1999) 11: 1603.]
Giehl K, Valenta R, Rothkegel M, Ronsiek M, Mannherz H-G and Jockusch BM (1994) Interaction of plant profilin with mammalian actin. Eur J Biochem 226: 681–689.
Hennessey ES, Drummond DR and Sparrow JC (1993) Molecular genetics of actin function. Biochem J 282: 657–671.
Janmey PA (1991) Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide. Methods Enzymol 196: 92–99.
Jiang C-J, Weeds AG and Hussey PJ (1997) The maize actin-depolymerizing factor, ZmADF3, redistributes to the growing tip of elongating root hairs and can be induced to translocate into the nucleus with actin. Plant J 12: 1035–1043.
Jiang C-J, Weeds AG, Khan S and Hussey PJ (1997) F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF). Proc Natl Acad Sci USA 94: 9973–9978.
Katakami Y, Katakami N, Janmey PA, Hartwig JH and Stossel TP (1992) Isolation of the phosphatidylinositol 4-monophosphate dissociable high-affinity profilin-actin complex. Biochim Biophys Acta 1122: 123–135.
Kulikova AL (1986) Quantity and forms of actin in conducting tissues of Heracleum sosnowskyi. Fiziologiya Rastenii 33: 481–487.
Kursanov AL, Kulikova AL and Turkina MV (1983) Actin-like protein from the phloem of Heracleum sosnowskyi. Physiol Vèg 21: 353–360.
Kwiatkowski DJ and Bruns GAP (1988) Human profilin. J Biol Chem 263: 5910–5915.
Liu X and Yen L-F (1992) Purification and characterization of actin from maize pollen. Plant Physiol 99: 1151–1155.
Lopez I, Anthony RG, Maciver SK, Jiang C-J, Khan S, Weeds AG and Hussey PJ (1996) Pollen specific expression of maize genes encoding actin depolymerizing factor-like proteins. Proc Natl Acad Sci 93: 7415–7420.
McCurdy DW and Williamson RE (1987) An actin-related protein inside pea chloroplasts. J Cell Sci 87: 449–456.
McCurdy DW and Williamson RE (1991) Actin and actin-associated proteins. In: Lloyd CW (ed.), The Cytoskeletal Basis of Plant Growth and Form. Academic Press Ltd, London, pp. 3–14.
Meagher RB (1991) Divergence and differential expression of actin gene families in higher plants. Int Rev Cytol 125: 139–163.
Meagher RB and McLean BG (1990) Diversity of plant actins. Cell Motil Cytoskel 16: 164–166.
Meagher RB and Williamson RE (1994) The plant cytoskeleton. In: Meyerowitz E, Somerville C (eds) Arabidopsis. Cold Spring Harbor Press, Cold Spring Harbor, NY, pp. 1049–1084.
Metcalf III TN, Szabo LJ, Schubert KR and Wang JL (1980) Immunochemical identification of an actin-like protein from soybean seedlings. Nature 285: 171–172.
Nefsky B and Bretscher A (1992) Yeast actin is relatively well behaved. Eur J Biochem. 206: 949–955.
Neuffer MG (1994) Growing maize for genetic studies. In: Freeling M, Walbot V (eds) The Maize Handbook. Springer-Verlag, New York, pp. 197–209.
Perelroizen I, Didry D, Christensen H, Chua N-H and Carlier M-F (1996) Role of nucleotide exchange and hydrolysis in the function of profilin in actin assembly. J Biol Chem 271: 12302–12309.
Ren H, Gibbon BC, Ashworth SL, Sherman DM, Yuan M and Staiger CJ (1997) Actin purified from maize pollen functions in living plant cells. Plant Cell 9: 1445–1457.
Rozycki M, Schutt CE and Lindberg U (1991) Affinity chromatography-based purification of profilin:actin. Methods Enzymol 196: 100–118.
Rubenstein PA (1990) The functional importance of multiple actin isoforms. Bioessays 12: 309–315.
Ruhlandt G, Lange U and Grolig F (1994) Profilins purified from higher plants bind to actin from cardiac muscle and to actin from a green alga. Plant Cell Physiol 35: 849–854.
Sambrook J, Fritsch EF and Maniatis T (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
Sheterline P, Clayton J and Sparrow JC (1998) Actin. Protein Profile 4: 1–272.
Staiger CJ, Gibbon BC, Kovar DR and Zonia LE (1997) Profilin and actin depolymerizing factor: modulators of actin organization in plants. Trends Plant Sci 2: 275–281.
Staiger CJ, Schliwa M (1987) Actin localization and function in higher plant cells. Protoplasma 141: 1–12.
Turkina MV, Kulikova AL, Sokolov OI, Bogatyrev VA and Kursanov AL (1987) Actin and myosin filaments from the conducting tissues of Heracleum sosnowskyi. Plant Physiol Biochem 25: 689–696.
Vahey M and Scordilis SP (1980) Contractile proteins from tomato. Can J Bot 58: 797–801.
Vahey M, Titus M, Trautwein R and Scordilis S (1982) Tomato actin and myosin: Contractile proteins from a higher land plant. Cell Motil 2: 131–147.
Vidali L and Hepler PK (1997) Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum. Cell Motil Cytoskel 36: 323–338.
Villanueva MA, Ho S-C and Wang JL (1990) Isolation and characterization of one isoform of actin from cultured soybean cells. Arch Biochem Biophys 277: 35–41.
Wegner A and Engel J (1975) Kinetics of the cooperative association of actin to actin filaments. Biophys Chem 3: 215–225.
Zechel K, Weber K (1978) Actins from mammals, bird, fish and slime mold characterized by isoelectric focusing in polyacrylamide gels. Eur J Biochem. 89: 105–112.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2000 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Staiger, C.J., Gibbon, B.C., Ren, H. (2000). Plant Actin Isolation and Characterization. In: Gelvin, S.B., Schilperoort, R.A. (eds) Plant Molecular Biology Manual. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4217-5_5
Download citation
DOI: https://doi.org/10.1007/978-94-011-4217-5_5
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-011-7655-2
Online ISBN: 978-94-011-4217-5
eBook Packages: Springer Book Archive