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J. Biochem, 1989, Vol. 106, No. 2 311-318
© 1989 Japanese Biochemical Society

research-article

A Fragmin-Like Protein from Plasmodium of Physarum polycephalum That Severs F-Actin and Caps the Barbed End of F-Actin in a Ca2+-Sensitive Way1

Kiyoshi Furuhashi2 and Sadashi Hatano

Department of Molecular Biology, Faculty of Science, Nagoya University Chikusa-ku, Nagoya, Aichi 464

2To whom correspondence should be addressed.

Many protein factors regulating actin polymerization can be extracted from plasmodia of Physarum polycephalum in the presence of a high EGTA concentration (30 mM). A protein factor with the molecular weight of 60, 000 (60 kDa protein) was especially interesting because of its fragmin-like properties. We purified and characterized this 60kDa protein in the present study. The purified 60 kDa protein enhanced the initial rate of G-actin polymerization, severed F-actin, and capped the barbed end of F-actin in a Ca2+-dependent way. The threshold concentration for Ca2+ was around 10–5M. The flow birefringence measurement showed that the length of F-actin decreased from 2.8 to 1.0 µm depending on the concentration of 60 kDa protein added to F-actin. These properties were identical to those of fragmin (Mr 42, 000) isolated from plasmodia (Hasegawa et al. (1980) Biochemistry 19, 2677–2683). However, the molecular weight, the tryptic peptide map, and the cross-reactivities with polyclonal anti-fragmin antibodies were different from those of fragmin. We concluded from these results that 60 kDa protein is a new Ca2+-sensitive F-actin-severing protein. Considering its similarity to fragmin, we termed the 60 kDa protein fragmin 60.

1This work was supported by a Grant-in-Aid (No. 6210500) from the Ministry of Education, Science and Culture of Japan.


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