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A myosin from a higher plant has structural similarities to class V myosins

Kinkema, Mark & Schiefelbein, John (1994) A myosin from a higher plant has structural similarities to class V myosins. Journal of Molecular Biology, 239(4), pp. 591-597.

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Abstract

In plant cells, myosin is believed to be the molecular motor responsible for actin-based motility processes such as cytoplasmic streaming and directed vesicle transport. In an effort to characterize plant myosin, a cDNA encoding a myosin heavy chain was isolated from Arabidopsis thaliana. The predicted product of the MYA1 gene is 173 kDa and is structurally similar to the class V myosins. It is composed of the highly-conserved NH2-terminal "head" domain, a putative calmodulin-binding "neck" domain an alpha-helical coiled-coil domain, and a COOH-terminal domain. Northern blot analysis shows that the Arabidopsis MYA1 gene is expressed in all the major plant tissues (flower, leaf, root, and stem). We suggest that the MYA1 myosin may be involved in a general intracellular transport process in plant cells.

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ID Code: 39096
Item Type: Journal Article
Additional URLs:
Keywords: myosin, Arabidopsis, cytoplasmic streaming
DOI: 10.1006/jmbi.1994.1400
ISSN: 0022-2836
Subjects: Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000) > PLANT BIOLOGY (060700) > Plant Cell and Molecular Biology (060702)
Divisions: Current > Research Centres > Centre for Tropical Crops and Biocommodities
Copyright Owner: Copyright 1994 Elsevier
Deposited On: 09 Dec 2010 14:38
Last Modified: 11 Aug 2011 03:17

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