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Is 2,3-butanedione monoxime an effective inhibitor of myosin-based activities in plant cells?

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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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Correspondence to David W. McCurdy.

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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

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