Summary
The effectiveness of 2,3-butanedione monoxime (BDM) as an inhibitor of plant myosins has been investigated. Three myosin-dependent motility phenomena in plants, namely cytoplasmic streaming inChara corallina, light-dependent chloroplast repositioning inElodea sp., and brefeldin A(BFA)-induced Golgi membrane dynamics in wheat (Triticum aestivum L. cv. Kite) roottip cells were investigated. All three processes were inhibited by the sulfhydryl-modifying agent N-ethylmalemide (NEM), indicating the probable involvement of myosin as the motor protein in each case. However, none of these myosin-dependent processes were inhibited by BDM at concentrations as high as 20 mM in some instances. These results therefore question the general usefulness of BDM as an inhibitor of myosin-based activities in plant cells.
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Abbreviations
- APW:
-
artificial pond water
- BDM:
-
2,3-butanedione monoxime
- BFA:
-
brefeldin A
- DMSO:
-
dimethyl sulfoxide
- MES:
-
2-(N-morpholino)ethanesulfonic acid
- NEM:
-
N-ethylmalemide
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McCurdy, D.W. Is 2,3-butanedione monoxime an effective inhibitor of myosin-based activities in plant cells?. Protoplasma 209, 120–125 (1999). https://doi.org/10.1007/BF01415707
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DOI: https://doi.org/10.1007/BF01415707