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J. Biochem, 2003, Vol. 133, No. 5 687-691
© 2003 Japanese Biochemical Society

CELL

Partial Specific Volume and Adiabatic Compressibility of G-Actin Depend on the Bound Nucleotide

Mahito Kikumoto+,§,1, Youjiro Tamura2, Atsushi Ooi3 and Koshin Mihashi,1

1 Department of Physics, Faculty of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602; 2 Department of Physics, Suzuka National College of Technology, Shiroko-cho, Suzuka, Mie 510-0294; and 3 Department of Sustainable Resource Sciences, Faculty of Bioresources, Mie University, Kamihama-cho 1515, Tsu, Mie 514-8507

We determined the partial specific volume and partial specific adiabatic compressibility of either ATP- or ADP-bound monomeric actin in the presence of Ca2+ by measuring the density of and sound velocity in a monomeric actin solution at 18°C. The partial specific volume of ATP-bound monomeric actin, equal to 0.744 cm3/g, which is exceptionally high among globular proteins, was reduced to 0.727 cm3/g when the tightly bound ATP was replaced with ADP. Associated with this, the adiabatic compressibility of ATP-bound monomeric actin, equal to 8.8 x 10–12 cm2/dyne, decreased to 5.8 x 10–12 cm2/dyne, which is a common value for globular proteins. These results suggested that an extraordinarily soft global conformation of ATP-bound monomeric actin is packed into a compact mass associated with the hydrolysis of bound ATP. When monomeric actin was limitedly proteolyzed at subdomain 2 with subtilisin, the nucleotide-dependent flexibility of the global conformation of monomeric actin was lost.

+ Present address: Protein Biophysics Group, KARC, CRL, Iwaoka 588-2, Iwaoka-cho, Nishi-ku, Kobe, Hyogo 651-2492.

§ To whom correspondence should be addressed: Tel: +81-0-78-969-2237 (direct-line), Fax: +81-0-78-969-2239, E-mail: kikumoto{at}crl.go.jp

Present address; Nihon Fukushi University, Faculty of Social and Information Sciences, Handa, Aichi 475-0012.


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