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Inhibitory Regulation of Higher-Plant Myosin by Ca2+
Ions1
Etsuo Yokota*,
Shoshi Muto, and
Teruo Shimmen
Department of Life Science, Faculty of Science, Himeji Institute of
Technology, Harima Science Park City, Hyogo 678-12, Japan (E.Y.,
T.S.); and BioScience Center, Nagoya University, Chikusa-ku,
Nagoya, 464-01, Japan (S.M.)
Myosin isolated from the pollen tubes
of lily (Lilium longiflorum) is composed of a 170-kD
heavy chain (E. Yokota and T. Shimmen [1994] Protoplasma 177:
153-162). Both the motile activity in vitro and the F-actin-stimulated
ATPase activity of this myosin were inhibited by Ca2+ at
concentrations higher than 10 6 M. In the
Ca2+ range between 106 and 105
M, inhibition of the motile activity was reversible. In
contrast, inhibition by more than 105 M
Ca2+ was not reversible upon Ca2+
removal. An 18-kD polypeptide that showed the same mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as that of
spinach calmodulin (CaM) was present in this myosin fraction. This
polypeptide showed a mobility shift in sodium dodecyl
sulfate-polyacrylamide gel electrophoresis in a
Ca2+-dependent manner. Furthermore, this polypeptide was
recognized by antiserum against spinach CaM. By immunoprecipitation
using antiserum against the 170-kD heavy chain, the 18-kD polypeptide was coprecipitated with the 170-kD heavy chain, provided that the
Ca2+ concentration was low, indicating that this 18-kD
polypeptide is bound to the 170-kD myosin heavy chain. However, the
18-kD polypeptide was dissociated from the 170-kD heavy chain at high Ca2+ concentrations, which irreversibly inhibited the
motile activity of this myosin. From these results, it is
suggested that the 18-kD polypeptide, which is likely to be CaM, is
associated with the 170-kD heavy chain as a light chain. It is also
suggested that this polypeptide is involved in the regulation of this
myosin by Ca2+. This is the first biochemical basis, to our
knowledge, for Ca2+ regulation of cytoplasmic streaming in
higher plants.
1
This work was supported by Grants-in-Aid for
Scientific Research (E.Y.) from the Ministry of Education, Science and
Culture of Japan (nos. 07740626 and 08740625).
*
Corresponding author; e-mail yokota{at}sci.himeji-tech.ac.jp; fax
81-7915-8-0175.
Plant Physiol. (1999) 119: 231-240
Copyright Clearance Center: 0032-0889/99/119//10
© 1999 American Society of Plant Physiologists
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