Evidence for structural differences between the two highly homologous actin-regulatory proteins, destrin and cofilin

Bioscience, Biotechnology and Biochemistry

Volumn 62, Issue 2, 1998, Pages 215-220

  Arima, Kazunari ^a   Imanaka, Minako ^a   Okuzono, Seigou ^a   Kazuta, Yasuaki ^a   Kotani, Susumu ^a  

^a KYUSHU INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Actin regulatory protein; Cofilin; Destrin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; CARRIER PROTEIN; CHYMOTRYPSIN; CYTOSKELETON PROTEIN; SUBTILISIN; TRYPSIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; GENE EXPRESSION; MOLECULAR GENETICS; PH; PLASMID; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ACTIN DEPOLYMERIZING FACTORS; ACTINS; AMINO ACID SEQUENCE; CARRIER PROTEINS; CHYMOTRYPSIN; CIRCULAR DICHROISM; CYTOSKELETAL PROTEINS; DESTRIN; GENE EXPRESSION; HYDROGEN-ION CONCENTRATION; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; SUBTILISINS; TRYPSIN;

EID: 0031992086     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.215     Document Type: Article

References (18)

1. E. Nishida, S. Maekawa, and H. Sakai, Biochemistry, 23, 5307-5313 (1984).
2. E. Nishida, E. Muneyuki, S. Maekawa, Y. Ohta, and H. Sakai, Biochemistry, 24, 6624-6630 (1985).
3. F. Matsuzaki, S. Matsumoto, I. Yahara, N. Yonezawa, E. Nishida, and H. Sakai, J. Biol. Chem., 263, 11564-11568 (1988).
4. K. Moriyama, E. Nishida, N. Yonezawa, H. Sakai, S. Matsumoto, K. Iida, and I. Yahara, J. Biol. Chem., 265, 5768-5737 (1990).
5. N. Yonezawa, E. Nishida, S. Maekawa, and H. Sakai, Biochem. J., 251, 121-127 (1988).
6. N. Yonezawa, E. Nishida, and H. Sakai, J. Biol. Chem., 260, 14410-14412 (1985).
7. K. Moriyama, N. Yonezawa, H. Sakai, I. Yahara, and E. Nishida, J. Biol. Chem., 267, 7240-7244 (1992).
8. K. B. Mullis and F. A. Faloona, Methods Enzymol., 155, 335-350 (1987).
9. F. Sanger, S. Nicklen, and A. R. Coulson, Proc. Natl. Acad. Sei. USA., 74, 5463-5467 (1977).
10. J. A. Spudich and S. Watt, J. Biol. Chem., 246, 4866-4871 (1971).
11. U. K. Laemmli, Nature, 227, 680-685 (1970).
12. H. Hirano, J. Prot. Chem., 8, 115-130 (1989).
13. Y. Fl. Chen, J. T. Young, and H. M. Martinez, Biochemistry, 11, 4120-4131 (1972).
14. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193, 265-275 (1951).
15. A. Fersht, in “Enzyme Structure and Mechanism,” 1st ed., ed. by W. H. Freeman and Company, San Francisco, 1977, pp. 2628.
16. N. Yonezawa, E. Nishida, K. Iida, H. Kumagai, I. Yahara, and H. Sakai, J. Biol. Chem., 266, 10485-10489 (1991).
17. H. Hatanaka, K. Ogura, K. Moriyama, S. Ichikawa, I. Yahara, and F. Inagaki, Cell, 85, 1047-1055 (1996).
18. C. Brenden and J. Tooze, in “Introduction to Protein Structure,” 1st ed., ed. by Garland Publishing, New York, 1991, pp. 247-251.