Further analysis of the role of spectrin repeat motifs in α-actinin dimer formation

European Biophysics Journal

Volumn 25, Issue 5-6, 1997, Pages 431-435

  Flood, G ^a   Rowe, A J ^a   Critchley, D R ^a   Gratzer, W B ^b  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

actinin; Dimer formation; Spectrin like repeats

Indexed keywords

ALPHA ACTININ;

ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; DIMERIZATION; DISSOCIATION CONSTANT; ESCHERICHIA COLI; PROTEIN FOLDING; PROTEIN STRUCTURE; SEDIMENTATION RATE; THERMOSTABILITY;

ACTININ; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CHICKENS; CIRCULAR DICHROISM; CLONING, MOLECULAR; DIMERIZATION; ESCHERICHIA COLI; HEAT; KINETICS; MUSCLE, SMOOTH; PROTEIN DENATURATION; RECOMBINANT FUSION PROTEINS; SPECTRIN; THERMODYNAMICS; ULTRACENTRIFUGATION;

ESCHERICHIA COLI; GALLUS GALLUS;

EID: 0030750630     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050057     Document Type: Article

References (25)

1. Blanchard A, Ohanian V, Critchley DR (1989) The structure and function of α-actinin. J Muscle Res Cell Motil 10:280-289
2. Davison MD, Critchley DR (1988) α-Actinins and DMD protein contain spectrin-like repeats. Cell 52:159-160
3. Emes CH, Rowe AJ (1978) Hydrodynamic studies on the self association of vertebrate skeletal muscle myosin. Biochem Biophys Acta 537:110-124
4. Flood G, Kahana E, Gilmore AP, Rowe AJ, Gratzer WB, Critchley DR (1995) Association of structural repeats in the α-actinin rod domain. Alignment of inter-subunit interactions. J Mol Biol 252:227-234
5. Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T (1992) Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 359:150-152
6. Gilbert LM, Gilbert GA (1973) Sedimentation velocity measurement of protein association. In: Hirs CHW, Timasheff SN (eds) Methods in enzymology. vol 27. Academic Press, New York, pp 273-296
7. Gilmore AP, Parr T, Patel B, Gratzer WB, Critchley DR (1994) Analysis of the phasing of the four spectrin-like repeats in α-actinin. Eur J Biochem 225:235-242
8. Greenfield N, Fasman GD (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4114
9. Harrington WF, Kegeles G (1973) Pressure effects in ultracentrifugation of interacting systems. In: Hirs CHW, Timasheff SN (eds) Methods in enzymology, vol 27. Academic Press, New York, pp 306-345
10. Imamura M, Endo T, Kuroda M, Tanaka T, Masaki T (1988) Substructure and higher structure of chicken smooth muscle α-actinin molecule. J Biol Chem 263:7800-7805
11. Imamura M, Masaki T (1992) A novel non-muscle α-actinin: purification and characterisation of chicken lung α-actinin. J Biol Chem 267:25927-25933
12. Kahana E, Gratzer WB (1991) Properties of the spectrin-like element of smooth-muscle α-actinin. Cell Motil Cytoskel 20:242-248
13. Kahana E, Marsh PJ, Henry AJ, Way M, Gratzer WB (1994) Conformation and phasing of dystrophin structural repeats. J Mol Biol 235:1271-1277
14. Kahana E, Gratzer WB (1995) Minimum folding unit of dystrophin rod domain. Biochemistry 34:8110-8114
15. Pascual J, Pfuhl M, Rivas G, Pastore A, Saraste M (1996) The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett 383:201-207
16. Perkins SJ (1986) Protein volumes and hydration effects. The calculation of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur J Biochem 157:169-180
17. Rallison JM, Harding SE (1985) Excluded volume for pairs of triaxial ellipsoids at dominant brownian motion. J Colloid Interface Sci 103:284-289
18. Smith DB, Johnson KS (1988) Single step purification of proteins expressed in E. coli as fusion proteins with glutathione-S-transferase. Gene 67:31-40
19. Speicher DW, Weglarz L, DeSilva TM (1992) Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J Biol Chem 267:14775-14782
20. Speicher DW, Marchesi VT (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311:177-180
21. Taylor KA, Taylor DW (1993) Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J Mol Biol 230:196-205
22. Ursitti JA, Kotula L, DeSilva TM, Curtis PJ, Speicher DW (1996) Mapping the human erythrocyte β-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the α-actinin dimer site. J Biol Chem 271:6636-6644
23. Viel A, Branton D (1994) Interchain binding at the tail end of the Drosophila spectrin molecule. Proc Natl Acad Sci USA 91: 10839-10843
24. Winograd E, Hume D, Branton D (1991) Phasing the conformational unit of spectrin. Proc Natl Acad Sci USA 88:10788-10791
25. Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D (1993) Crystal structure of the repetitive segments of spectrin. Science 262:2027-2030