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  • 1
    Electronic Resource
    Electronic Resource
    Calcium-dependent protein kinase in the green alga Chara (1992)
    Springer
    Planta 188 (1992), S. 54-61 
    Details
    ISSN: 1432-2048
    Keywords: Actin ; Chara (protein kinase) ; Cytoplasmic streaming ; Myosin ; Protein kinase (calcium dependent)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytoplasmic streaming in the characean algae is inhibited by micromolar rises in the level of cytosolic free Ca2+, but both the mechanism of action and the molecular components involved in this process are unknown. We have used monoclonal antibodies against soybean Ca2+-dependent protein kinase (CDPK), a kinase that is activated by micromolar Ca2+ and co-localizes with actin filaments in higher-plant cells (Putnam-Evans et al., 1989, Cell Motil. Cytoskel. 12, 12–22) to identify and localize its characean homologue. Immunoblot analysis revealed that CDPK in Chara corralina Klein ex. Wild shares the same relative molecular mass (51–55 kDa) as the kinase purified from soybean, and after electrophoresis in denaturing gels is capable of phosphorylating histone III-S in a Ca2+-dependent manner. Immunofluorescence microscopy localized CDPK in Chara to the subcortical actin bundles and the surface of small organelles and other membrane components of the streaming endoplasm. The endoplasmic sites carrying CDPK were extracted from internodal cells by vacuolar perfusion with 1 mM ATP or 10−4 M Ca2+. Both the localization of CDPK and its extraction from internodal cells by perfusion with ATP or high Ca2+ are properties similar to that reported for the heavy chain of myosin in Chara (Grolig et al., 1988, Eur. J. Cell Biol. 47, 22–31). Based on its endoplasmic location and inferred enzymatic properties, we suggest that CDPK may be a putative element of the signal-transduction pathway that mediates the rapid Ca2+-induced inhibition of streaming that occurs in the characean algae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198939
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  • 2
    Electronic Resource
    Electronic Resource
    Calcium-dependent protein kinase in the green algaChara (1992)
    Springer
    Planta 188 (1992), S. 54-61 
    Details
    ISSN: 1432-2048
    Keywords: Actin ; Chara (protein kinase) ; Cytoplasmic streaming ; Myosin ; Protein kinase (calcium dependent)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytoplasmic streaming in the characean algae is inhibited by micromolar rises in the level of cytosolic free Ca2+, but both the mechanism of action and the molecular components involved in this process are unknown. We have used monoclonal antibodies against soybean Ca2+-dependent protein kinase (CDPK), a kinase that is activated by micromolar Ca2+ and co-localizes with actin filaments in higher-plant cells (Putnam-Evans et al., 1989, Cell Motil. Cytoskel.12, 12–22) to identify and localize its characean homologue. Immunoblot analysis revealed that CDPK inChara corralina Klein ex. Wild shares the same relative molecular mass (51–55 kDa) as the kinase purified from soybean, and after electrophoresis in denaturing gels is capable of phosphorylating histone III-S in a Ca2+-dependent manner. Immunofluorescence microscopy localized CDPK inChara to the subcortical actin bundles and the surface of small organelles and other membrane components of the streaming endoplasm. The endoplasmic sites carrying CDPK were extracted from internodal cells by vacuolar perfusion with 1 mM ATP or 10−4 M Ca2+. Both the localization of CDPK and its extraction from internodal cells by perfusion with ATP or high Ca2+ are properties similar to that reported for the heavy chain of myosin inChara (Grolig et al., 1988, Eur. J. Cell Biol.47, 22–31). Based on its endoplasmic location and inferred enzymatic properties, we suggest that CDPK may be a putative element of the signal-transduction pathway that mediates the rapid Ca2+-induced inhibition of streaming that occurs in the characean algae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01160712
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  • 3
    Electronic Resource
    Electronic Resource
    Reorganization of cortical actin microfilaments and microtubules at preprophase and mitosis in wheat root-tip cells: A double label immunofluorescence study (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 15 (1990), S. 76-87 
    Details
    ISSN: 0886-1544
    Keywords: antiactin ; cytochalasin B ; plant cytoskeleton ; tubulin ; oryzalin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Following our recent description [McCurdy et al.: Protoplasma. 147:204-206, 1988] of arrays of transverse cortical microfilaments (MFs) in preprophase roottip cells of wheat (Triticum aestivum L. cv. Kite), we have performed double label immunofluorescence microscopy to correlate the formation of these arrays with the known rearrangement of cortical microtubules (MTs) that occurs during preprophase. At early preprophase, indicated by a broad (i.e., young) preprophase band (PPB) of MTs, actin MFs are transverse only in the central region of the cell cortex. By late preprophase, however, cells that possess a mature (i.e., narrow) PPB of MTs have arrays of transverse MFs that occupy the entire cortical surface of the cell. Thus, apart from the PPB zone, the transverse MFs in these arrays do not colocalize with transverse cortical MTs. Depolymerization of MTs using the herbicide oryzalin does not effect the arrays of cortical MFs; however, experiments using cytochalasin B in combination with oryzalin indicate that cellular MTs are necessary for the formation of the arrays of transverse cortical MFs. The arrays of cortical MFs disintegrate during prophase into short fragments of random, filamentous actin. This situation persists until the completion of cytokinesis. The absence of MFs during mitosis in densely-cytoplasmic meristematic cells of wheat root tips indicates that filamentous actin may not have a universal function in plant cell division. The possible function of the arrays of cortical MFs in preprophase cells is discussed.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970150204
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of cytochalasins on actin in dividing root tip cells of Allium and Triticum: A comparative immunocytochemical study (1991)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 18 (1991), S. 107-112 
    Details
    ISSN: 0886-1544
    Keywords: cell division ; cytoskeleton ; root cell ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A collaborative effort was initiated to resolve differences in two recent papers on the effects of cytochalasins in root cells. While both studies reported similar effects on interphase cells (i.e., replacement of microfilaments by many small specks and rods), Palevitz (Cell Motil. Cytoskeleton 9:283-298, 1988) maintained that cytochalasins B and D induce actin aggregation at the poles of dividing Allium root cells at a concentration of 10 μM with rhodamine phalloidin as a reporter probe, whereas McCurdy and Gunning (Cell Motil. Cytoskeleton 15:76-87, 1990) could not find these aggregates following antiactin immunocytochemistry in Triticum roots treated with CB at 50 μM. Employing identical methods and materials in the same laboratory, we found that CD induces polar actin aggregates in dividing cells of both species. However, the aggregates in Triticum are smaller and occur less frequently than those in Allium. A similar pattern is seen with CB.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970180205
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  • 5
    Electronic Resource
    Electronic Resource
    Actin dynamics during the cell cycle in Chlamydomonas reinhardtii (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 117-126 
    Details
    ISSN: 0886-1544
    Keywords: algae ; cell division ; cytokinesis ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have used two monoclonal antibodies to demonstrate the presence and localization of actin in interphase and mitotic vegetative cells of the green alga Chlamydomonas reinhardtii. Commercially available monoclonal antibodies raised against smooth muscle actin (Lessard: Cell Motil. Cytoskeleton 10:349-362, 1988; Lin: Proc. Natl. Acad. Sci. USA 78:2335-2339, 1981) identify Chlamydomonasactin as a ∼43,000-Mr protein by Western immunoblot procedures. In an earlier study, Detmers and coworkers (Cell Motil. 5:415-430, 1985) first identified Chlamydomonas actin using NBD-phallacidin and an antibody raised against Dictyostelium actin; they demonstrated that F-actin is localized in the fertilization tubule of mating gametes. Here, we show by immunofluorescence that vegetative Chlamydomonas cells have an array of actin that surrounds the nucleus in interphase cells and undergoes dramatic reorganization during mitosis and cytokinesis. This includes the following: reorganization of actin to the ante- rior of the cell during preprophase; the formation of a cruciate actin band in prophase; reorganization to a single anterior actin band in metaphase; rearrange- ment forming a focus of actin anterior to the metaphase plate; reextension of the actin band in anaphase; presence of actin in the forming cleavage furrow during telophase and cytokinesis; and finally reestablishment of the interphase actin array. The studies presented here do not allow us to discriminate between G and F-actin. None the less, our observations, demonstrating dynamic reorganization of actin during the cell cycle, suggest a role for actin that may include the movement of basal bodies toward the spindle poles in mitosis and the formation of the cleavage furrow during cytokinesis. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970220205
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  • 6
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    Calcium-dependent protein kinase in the green algaChara (1992)
    Springer
    Details
    Publication Date: 1992-01-01
    Print ISSN: 0032-0935
    Electronic ISSN: 1432-2048
    Topics: Biology
    Published by Springer
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