Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo

Biochemical Journal

Volumn 385, Issue 1, 2005, Pages 29-36

  Sal Man, Neta ^a   Shai, Yechiel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Assembly; Peptide; Positively charged residues; Tar receptor; Transmembrane domain

Indexed keywords

AMINO ACIDS; DIMERIZATION; DISEASES; ESCHERICHIA COLI; GENETIC ENGINEERING; SYNTHESIS (CHEMICAL);

ARGININE MUTATIONS; GENETIC DISEASES; MUTATIONS; TRANSMEMBRANES;

PROTEINS;

AMINO ACID; AMINO ACID RECEPTOR; ARGININE; ASPARTIC ACID; DNA; MEMBRANE PROTEIN; MUTANT PROTEIN; SYNTHETIC PEPTIDE; TAR 1 PEPTIDE; TAR RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; BIOSENSOR; CHIMERA; CIRCULAR DICHROISM; DIMERIZATION; DNA SEQUENCE; ESCHERICHIA COLI; GENE MUTATION; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SPECTROSCOPY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ARGININE; CELL MEMBRANE; DIMERIZATION; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMINO ACID; RECOMBINANT FUSION PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 12744255176     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041022     Document Type: Article

References (33)

1. Ding, P. Z. and Wilson, T. H. (2001) The effect of modifications of the charged residues in the transmembrane helices on the transport activity of the melibiose carrier of Escherichia coli. Biochem. Biophys. Res. Commun. 285, 348-354
2. Burnay, M., Crambert, G., Kharoubi-Hess, S., Geering, K. and Horisberger, J. D. (2003) Electrogenicity of Na,K- and H,K-ATPase activity and presence of a positively charged amino acid in the fifth transmembrane segment. J. Biol. Chem. 278, 19237-19244
3. 189 in transporter function. J. Biol. Chem. 275, 7117-7124
4. Partridge, A. W., Melnyk, R. A. and Deber, C. M. (2002) Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment. Biochemistry 41, 3647-3653
5. Partridge, A. W., Therien, A. G. and Deber, C. M. (2004) Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease. Proteins 54, 648-656
6. +-ATPase gamma-subunit. Nat. Genet. 26, 265-266
7. Therien, A. G. and Deber, C. M. (2002) Oligomerization of a peptide derived from the transmembrane region of the sodium pump gamma subunit: effect of the pathological mutation G41R. J. Mol. Biol. 322, 583-590
8. Langosch, D., Brosig, B., Kolmar, H. and Fritz, H. J. (1996) Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263, 525-530
9. Scott, W. G., Milligan, D. L., Milburn, M. V., Prive, G. G., Yeh, J., Koshland, Jr, D. E. and Kim, S. H. (1993) Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. J. Mol. Biol. 232, 555-573
10. Milburn, M. V., Prive, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, Jr, D. E. and Kim, S. H. (1991) Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254, 1342-1347
11. Kim, K. K., Yokota, H. and Kim, S. H. (1999) Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature (London) 400, 787-792
12. Gerstein, M. and Chothia, C. (1999) Perspectives: signal transduction. Proteins in motion. Science 285, 1682-1683
13. Pakula, A. A. and Simon, M. I. (1992) Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor. Proc. Natl. Acad. Sci. U.S.A. 89, 4144-4148
14. Sal-Man, N., Gerber, D. and Shai, Y. (2004) The composition rather than position of polar residues (QxxS) drives aspartate receptor transmembrane domain dimerization in vivo. Biochemistry 43, 2309-2313
15. Melnyk, R. A., Partridge, A. W. and Deber, C. M. (2001) Retention of native-like oligomerization states in transmembrane segment peptides: application to the Escherichia coli aspartate receptor. Biochemistry 40, 11106-11113
16. Oosawa, K. and Simon, M. (1986) Analysis of mutations in the transmembrane region of the aspartate chemoreceptor in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 83, 6930-6934
17. Lemmon, M. A., Flanagan, J. M., Hunt, J. F., Adair, B. D., Bormann, B. J., Dempsey, C. E. and Engelman, D. M. (1992) Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices. J. Biol. Chem. 267, 7683-7689
18. Lemmon, M.A., Treutlein, H. R., Adams, P. D., Brunger, A. T. and Engelman, D. M. (1994) A dimerization motif for transmembrane alpha-helices. Nat. Struct. Biol. 1, 157-163
19. Gerber, D., Sal-Man, N. and Shai, Y. (2004) Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization. J. Biol. Chem. 279, 21177-21182
20. Brosig, B. and Langosch, D. (1998) The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues. Protein Sci. 7, 1052-1056
21. Han, X. and Tamm, L. K. (2000) A host-guest system to study structure-function relationships of membrane fusion peptides. Proc. Natl. Acad. Sci. U.S.A. 97, 13097-13102
22. Gerber, D. and Shai, Y. (2001) In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane. J. Biol. Chem. 276, 31229-31232
23. Eckert, D. M., Malashkevich, V. N., Hong, L. H., Carr, P. A. and Kim, P. S. (1999) Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99, 103-115
24. Wu, C. S., Ikeda, K. and Yang, J. T. (1981) Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20, 566-570
25. Greenfield, N. and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116
26. Mendrola, J. M., Berger, M. B., King, M. C. and Lemmon, M. A. (2002) The single transmembrane domains of ErbB receptors self-associate in cell membranes. J. Biol. Chem. 277, 4704-4712
27. McGaughey, G. B., Gagne, M. and Rappe, A. K. (1998) pi-Stacking interactions. Alive and well in proteins. J. Biol. Chem. 273, 15458-15463
28. Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77-83
29. Gratkowski, H., Lear, J. D. and DeGrado, W. F. (2001) Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. U.S.A. 98, 880-885
30. Zhou, F. X., Merianos, H. J., Brunger, A. T. and Engelman, D. M. (2001) Polar residues drive association of polyleucine transmembrane helices. Proc. Natl. Acad. Sci. U.S.A. 98, 2250-2255
31. Manolios, N., Letourneur, F., Bonifacino, J. S. and Klausner, R. D. (1991) Pairwise, cooperative and inhibitory interactions describe the assembly and probable structure of the T-cell antigen receptor. EMBO J. 10, 1643-1651
32. Ruan, W., Lindner, E. and Langosch, D. (2004) The interface of a membrane-spanning leucine zipper mapped by asparagine-scanning mutagenesis. Protein Sci. 13, 555-559
33. Umemura, T., Tatsuno, I., Shibasaki, M., Homma, M. and Kawagishi, I. (1998) Intersubunit interaction between transmembrane helices of the bacterial aspartate chemoreceptor homodimer. J. Biol. Chem. 273, 30110-30115