Structural and functional analysis of transmembrane segment IV of the salt tolerance protein Sod2

Journal of Biological Chemistry

Volumn 288, Issue 34, 2013, Pages 24609-24624

  Ullah, Asad ^a   Kemp, Grant ^a   Lee, Brian ^a   Alves, Claudia ^a   Young, Howard ^a   Sykes, Brian D ^a   Fliegel, Larry ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE MUTATIONS; ALANINE-SCANNING MUTAGENESIS; AMINO ACID RESIDUES; CATION TRANSPORTS; CONFORMATIONAL CHANGE; MUTANT PROTEINS; SCHIZOSACCHAROMYCES POMBE; TRANSMEMBRANE SEGMENTS;

AMINO ACIDS; CELL MEMBRANES; ESCHERICHIA COLI; LITHIUM; MAMMALS; MUTAGENESIS; POSITIVE IONS; SENSITIVITY ANALYSIS;

PROTEINS;

ESCHERICHIA COLI PROTEIN; LITHIUM; MUTANT PROTEIN; PROTEIN NHAA; PROTEIN SOD2; SCHIZOSACCHAROMYCES POMBE PROTEIN; SODIUM; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ESCHERICHIA COLI; GENE MUTATION; MAMMAL; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SALT TOLERANCE; SCHIZOSACCHAROMYCES POMBE; STRUCTURAL HOMOLOGY; ZYGOSACCHAROMYCES ROUXII;

ALANINE SCANNING MUTAGENESIS; CATION COORDINATION; MEMBRANE FUNCTION; MEMBRANE PROTEINS; NA+/H+ EXCHANGER; NUCLEAR MAGNETIC RESONANCE; SALT TOLERANCE; SODIUM TRANSPORT; SODIUM/PROTON EXCHANGE;

AMINO ACID SUBSTITUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FUNGAL PROTEINS; MUTATION, MISSENSE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; SODIUM-HYDROGEN ANTIPORTER; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84883176594     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.483065     Document Type: Article

References (65)

1. + antiporter confers sodium and lithium tolerance in fission yeast. EMBO J. 11, 1631-1640
2. Haworth, R. S., Lemire, B. D., Crandall, D., Cragoe, E. J., Jr., and Fliegel, L. (1991) Characterization of proton fluxes across the cytoplasmic membrane of the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1098, 79-89
3. + exchanger of fission yeast. Biochemistry 37, 8282-8288
4. + exchanger of Schizosaccharomyces pombe. Biochim. Biophys. Acta 1788, 983-992
5. Brett, C. L., Donowitz, M., and Rao, R. (2005) Evolutionary origins of eukaryotic sodium/proton exchangers. Am. J. Physiol. Cell Physiol. 288, C223-C239
6. + antiporter and insights into mechanism of action and regulation by pH. Nature 435, 1197-1202
7. + antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension. Proc. Natl. Acad. Sci. U.S.A. 104, 18677-18681
8. Schushan, M., Xiang, M., Bogomiakov, P., Padan, E., Rao, R., and Ben-Tal, N. (2010) Model-guided mutagenesis drives functional studies of human NHA2, implicated in hypertension. J. Mol. Biol. 396, 1181-1196
9. + exchanger isoform 1. J. Biol. Chem. 281, 29817-29829
10. + exchanger. J. Biol. Chem. 284, 11546-11556
11. + exchanger. Biochim. Biophys. Acta 1788, 2481-2488
12. + exchanger isoform 1 (NHE1) using the divide and conquer approach. Biochem. Cell Biol. 89, 189-199
13. + exchanger. J. Biol. Chem. 283, 22018-22030
14. + exchanger. Biochem. J. 401, 623-633
15. + exchanger. J. Biol. Chem. 285, 36656-36665
16. + exchanger. J. Biol. Chem. 280, 17863-17872
17. + exchanger that are important for proton translocation. Mol. Cell. Biochem. 254, 117-124
18. + exchanger of Schizosaccharomyces pombe. Mol. Cell. Biochem. 268, 83-92
19. + exchanger Sod2 of the fission yeast Schizosaccharomyces pombe. Can J. Physiol. Pharmacol. 83, 565-572
20. + exchanger isoform 1. Biochem. J. 379, 31-38
21. + exchanger in human choriocarcinoma (BeWo) cells. Pflugers Arch. 433, 792-802
22. + exchanger expression in fetal and neonatal mice. Am. J. Physiol. Heart Circ. Physiol. 283, H273-H283
23. Dibrov, P., Smith, J. J., Young, P. G., and Fliegel, L. (1997) Identification and localization of the sod2 gene product in fission yeast. FEBS Lett. 405, 119-124
24. 2+-ATPase regulatory proteins for high-resolution structural studies. Protein Expr. Purif. 40, 118-125
25. Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665
26. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR 4, 845-858
27. α) coupling-constants in N-15-enriched proteins. J. Am. Chem. Soc. 115, 7772-7777
28. β J couplings in isotopically enriched proteins. J. Am. Chem. Soc. 117, 5312-5315
29. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
30. Johnson, B. A., and Blevins, R. A. (1994) NMRView: a computer program for the visualization and analysis of NMRdata. J. Biomol. NMR4, 603-614
31. Schwieters, C. D., Kuszewski, J. J., Tjandra, N., and Clore, G. M. (2003) The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160, 65-73
32. Eswar, N., Webb, B., Marti-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M. Y., Pieper, U., and Sali, A. (2006) Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics Chapter 5, Unit 5.6
33. Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., Thompson, J. D., and Higgins, D. G. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539
34. Goujon, M., McWilliam, H., Li, W., Valentin, F., Squizzato, S., Paern, J., and Lopez, R. (2010) A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res. 38, W695-W699
35. Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
36. Cole, C., Barber, J. D., and Barton, G. J. (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 36, W197-W201
37. Bhattacharya, A., Tejero, R., and Montelione, G. T. (2007) Evaluating protein structures determined by structural genomics consortia. Proteins 66, 778-795
38. Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., and Ben-Tal, N. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33, W299-W302
39. Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164
40. Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
41. + exchangers. Biochem. J. 357, 1-10
42. + antiporter. Proc. Natl. Acad. Sci. U.S.A. 97, 6896-6901
43. + exchanger. Eur. J. Biochem. 268, 4674-4685
44. + antiport? FEBS Lett. 424, 1-5
45. Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., and Sykes, B. D. (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5, 67-81
46. + exchanger isoform 1. Channels 2, 329-336
47. + antiporter. Trends Biochem. Sci. 33, 435-443
48. Fleming, K. G., and Engelman, D. M. (2001) Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proc. Natl. Acad. Sci. U.S.A. 98, 14340-14344
49. - conformation. Biophys. J. 79, 2754-2760
50. Padan, E., Kozachkov, L., Herz, K., and Rimon, A. (2009) NhaA crystal structure: functional-structural insights. J. Exp. Biol. 212, 1593-1603
51. +/glucose cotransporter. J. Biol. Chem. 276, 49188-49194
52. + exchanger are involved in the transport and selection of cations. J. Biol. Chem. 279, 812-819
53. Li, H., and Pajor, A. M. (2003) Serines 260 and 288 are involved in sulfate transport by hNaSi-1. J. Biol. Chem. 278, 37204-37212
54. + antiporters. Mol. Membr. Biol. 23, 349-361
55. Cunningham, F., and Deber, C. M. (2007) Optimizing synthesis and expression of transmembrane peptides and proteins. Methods 41, 370-380
56. Hunt, J. F., Earnest, T. N., Bousché, O., Kalghatgi, K., Reilly, K., Horváth, C., Rothschild, K. J., and Engelman, D. M. (1997) A biophysical study of integral membrane protein folding. Biochemistry 36, 15156-15176
57. Katragadda, M., Alderfer, J. L., and Yeagle, P. L. (2001) Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Biophys. J. 81, 1029-1036
58. Katragadda, M., Chopra, A., Bennett, M., Alderfer, J. L., Yeagle, P. L., and Albert, A. D. (2001) Structures of the transmembrane helices of the Gprotein coupled receptor, rhodopsin. J. Pept. Res. 58, 79-89
59. Hu, N. J., Iwata, S., Cameron, A. D., and Drew, D. (2011) Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 478, 408-411
60. Cordes, F. S., Bright, J. N., and Sansom, M. S. (2002) Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323, 951-960
61. Screpanti, E., and Hunte, C. (2007) Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159, 261-267
62. + antiporter of Escherichia coli. Biochemistry 41, 609-617
63. Oberai, A., Ihm, Y., Kim, S., and Bowie, J. U. (2006) A limited universe of membrane protein families and folds. Protein Sci. 15, 1723-1734
64. + exchanger 1 (NHE1): functional and clinical implications. J. Biol. Chem. 282, 37854-37863
65. Pace, C. N., and Scholtz, J. M. (1998) A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75, 422-427