67 research outputs found

    Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array

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    Metazoan cells harness the power of actin dynamics to create cytoskeletal arrays that stimulate protrusions and drive intracellular organelle movements. In plant cells, the actin cytoskeleton is understood to participate in cell elongation; however, a detailed description and molecular mechanism(s) underpinning filament nucleation, growth, and turnover are lacking. Here, we use variable-angle epifluorescence microscopy (VAEM) to examine the organization and dynamics of the cortical cytoskeleton in growing and nongrowing epidermal cells. One population of filaments in the cortical array, which most likely represent single actin filaments, is randomly oriented and highly dynamic. These filaments grow at rates of 1.7 µm/s, but are generally short-lived. Instead of depolymerization at their ends, actin filaments are disassembled by severing activity. Remodeling of the cortical actin array also features filament buckling and straightening events. These observations indicate a mechanism inconsistent with treadmilling. Instead, cortical actin filament dynamics resemble the stochastic dynamics of an in vitro biomimetic system for actin assembly

    Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array

    Get PDF
    Metazoan cells harness the power of actin dynamics to create cytoskeletal arrays that stimulate protrusions and drive intracellular organelle movements. In plant cells, the actin cytoskeleton is understood to participate in cell elongation; however, a detailed description and molecular mechanism(s) underpinning filament nucleation, growth, and turnover are lacking. Here, we use variable-angle epifluorescence microscopy (VAEM) to examine the organization and dynamics of the cortical cytoskeleton in growing and nongrowing epidermal cells. One population of filaments in the cortical array, which most likely represent single actin filaments, is randomly oriented and highly dynamic. These filaments grow at rates of 1.7 µm/s, but are generally short-lived. Instead of depolymerization at their ends, actin filaments are disassembled by severing activity. Remodeling of the cortical actin array also features filament buckling and straightening events. These observations indicate a mechanism inconsistent with treadmilling. Instead, cortical actin filament dynamics resemble the stochastic dynamics of an in vitro biomimetic system for actin assembly

    Spektrum - 3/2006

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    The tomato cis– prenyltransferase gene family

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    Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/1/tpj12063-sup-0004-FigureS4.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/2/tpj12063-sup-0005-FigureS5.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/3/tpj12063-sup-0002-FigureS2.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/4/tpj12063-sup-0003-FigureS3.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/5/tpj12063-sup-0001-FigureS1.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/6/tpj12063.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/96709/7/tpj12063-sup-0006-TableS1.pd

    The ER luminal C‐terminus of AtSec62 is critical for male fertility and plant growth in Arabidopsis thaliana

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    Protein translocation into the endoplasmic reticulum (ER) occurs either co‐ or post‐translationally through the Sec translocation system. The Arabidopsis Sec post‐translocon is composed of the protein‐conducting Sec61 complex, the chaperone‐docking protein AtTPR7, the J‐domain‐containing proteins AtERdj2A/B and the yet uncharacterized AtSec62. Yeast Sec62p is suggested to mainly function in post‐translational translocation, whereas mammalian Sec62 also interacts with ribosomes. In Arabidopsis, loss of AtSec62 leads to impaired growth and drastically reduced male fertility indicating the importance of AtSec62 in protein translocation and subsequent secretion in male gametophyte development. Moreover, AtSec62 seems to be divergent in function as compared with yeast Sec62p, since we were not able to complement the thermosensitive yeast mutant sec62‐ts. Interestingly, AtSec62 has an additional third transmembrane domain in contrast to its yeast and mammalian counterparts resulting in an altered topology with the C‐terminus facing the ER lumen instead of the cytosol. In addition, the AtSec62 C‐terminus has proven to be indispensable for AtSec62 function, since a construct lacking the C‐terminal region was not able to rescue the mutant phenotype in Arabidopsis. We thus propose that Sec62 acquired a unique topology and function in protein translocation into the ER in plants
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