Functional reassembly of the anion transport domain of human red cell band 3 (AE1) from multiple and non-complementary fragments

FEBS Letters

Volumn 433, Issue 3, 1998, Pages 223-227

  Groves, Jonathan D ^a   Wang, Lin ^a,b   Tanner, Michael J A ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Anion exchanger; Band 3 protein; Chloride transport; Heterologous expression; Membrane protein fragment; Xenopus oocyte

Indexed keywords

COMPLEMENTARY DNA; ERYTHROCYTE BAND 3 PROTEIN; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; BINDING SITE; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; ERYTHROCYTE MEMBRANE; FEMALE; GENETICS; HUMAN; METABOLISM; MOLECULAR CLONING; OOCYTE; POLYMERASE CHAIN REACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; XENOPUS LAEVIS;

ANIMALS; ANION EXCHANGE PROTEIN 1, ERYTHROCYTE; BINDING SITES; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ERYTHROCYTE MEMBRANE; FEMALE; HUMANS; MODELS, MOLECULAR; OOCYTES; PEPTIDE FRAGMENTS; POLYMERASE CHAIN REACTION; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; XENOPUS LAEVIS;

EID: 0032555375     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)00909-0     Document Type: Article

References (22)

1. Jennings, M.L. (1989) Annu. Rev. Biophys. Biophys. Chem. 18, 397-430.
2. Reithmeier, R.A.F. (1993) Curr. Opin. Struct. Biol. 3, 515-523.
3. Tanner, M.J.A. (1997) Mol. Membr. Biol. 14, 155-165.
4. Low, P.S. (1986) Biochim. Biophys. Acta 864, 145-167.
5. Lepke, S. and Passow, H. (1976) Biochim. Biophys. Acta 455, 353-370.
6. Lepke, S., Becker, A. and Passow, H. (1992) Biochim. Biophys. Acta 1106, 13-16.
7. Groves, J.D. and Tanner, M.J.A. (1992) J. Biol. Chem. 267, 22163-22170.
8. Popov, M., Tam, L.Y., Li, J. and Reithmeier, R.A.F. (1997) J. Biol. Chem. 272, 18325-18332.
9. Oikawa, K., Lieberman, D.M. and Reithmeier, R.A.F. (1985) Biochemistry 24, 2843-2848.
10. Wang, D.N., Sarabia, V.E., Reithmeier, R.A.F. and Kühlbrandt, W. (1994) EMBO J. 13, 3230-3235.
11. Groves, J.D. and Tanner, M.J.A. (1995) J. Biol. Chem. 270, 9097-9105.
12. Wang, L., Groves, J.D., Mawby, W.J. and Tanner, M.J.A. (1997) J. Biol. Chem. 272, 10631-10638.
13. Kobilka, B.K., Kobilka, T.S., Daniel, K., Regan, J.W., Caron, M.G. and Lefkowitz, R.J. (1988) Science 240, 1310-1316.
14. Bibi, E. and Kaback, H.R. (1990) Proc. Natl. Acad. Sci. USA 87, 4325-4329.
15. Ridge, K.D., Lee, S.J. and Abdulaev, N.G. (1996) J. Biol. Chem. 271, 7860-7867.
16. Popot, J.-L. and Engelman, D.M. (1990) Biochemistry 29, 4031-4037.
17. Groves, J.D., Wang, L. and Tanner, M.J.A. (1998) Biochem. J. 332, 161-171.
18. Groves, J.D. and Tanner, M.J.A. (1994) Mol. Membr. Biol. 11, 31-38.
19. Laemmli, U.X. (1970) Nature 227, 680-681.
20. Schägger, H. and von Jagow, G. (1987) Biochemistry 166, 368-379.
21. Groves, J.D. and Tanner, M.S.A. (1994) J. Membr. Biol. 140, 81-88.
22. Bruee, L.J., Cope, D.L., Jones, G.K., Schofield, A.E., Burley, M., Povey, S., Unwin, R.J., Wrong, O. and Tanner, M.J.A. (1997) J. Clin. Invest. 100, 1693-1707.