The C-terminal segment of yeast BMH proteins exhibits different structure compared to other 14-3-3 protein isoforms

Biochemistry

Volumn 49, Issue 18, 2010, Pages 3853-3861

  Veisova, Dana ^a   Rezabkova, Lenka ^a,b   Stepanek, Miroslav ^b   Novotna, Pavlina ^c   Herman, Petr ^b   Vecer, Jaroslav ^b   Obsil, Tomas ^a,b   Obsilova, Veronika ^a  

^a INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c INSTITUTE OF CHEMICAL TECHNOLOGY   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

14-3-3 PROTEINS; BIOPHYSICAL TECHNIQUES; C-TERMINAL SEGMENTS; C-TERMINAL TAIL; CONFORMATIONAL BEHAVIOR; DIFFERENT STRUCTURE; ISOFORMS; LIGAND BINDING; MOLECULAR SIZE; POLYGLUTAMINE; SEDIMENTATION ANALYSIS; SEDIMENTATION VELOCITIES; STRUCTURAL CHANGE; TIME RESOLVED FLUORESCENCE ANISOTROPY; TIME-RESOLVED; TRYPTOPHAN FLUORESCENCE;

AMINO ACIDS; BIOLOGICAL MEMBRANES; CONFORMATIONS; FLUORESCENCE; LIGANDS; OLIGOMERS; SIZE EXCLUSION CHROMATOGRAPHY; YEAST;

PROTEINS;

DIMER; FUNGAL PROTEIN; ISOPROTEIN; POLYGLUTAMINE; PROTEIN 14 3 3; PROTEIN BMH1; PROTEIN BMH2; TRYPTOPHAN; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EUKARYOTE; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; LIGAND BINDING; LIGHT SCATTERING; MOLECULAR SIZE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEDIMENTATION;

14-3-3 PROTEINS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; DIMERIZATION; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT;

EUKARYOTA;

EID: 77951881101     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100273k     Document Type: Article

References (25)

1. Fu, H., Subramanian, R. R., and Masters, S. C. (2000) 14-3-3 proteins: structure, function, and regulation Annu. Rev. Pharmacol. Toxicol. 40, 617-647
2. Mackintosh, C. (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes Biochem. J. 381, 329-342
3. Aitken, A. (2006) 14-3-3 proteins: A historic overview Semin. Cancer Biol. 16, 162-172 (Pubitemid 43796128)
4. Xiao, B., Smerdon, S. J., Jones, D. H., Dodson, G. G., Soneji, Y., Aitken, A., and Gamblin, S. J. (1995) Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways Nature 376, 188-191
5. Muslin, A. J., Tanner, J. W., Allen, P. M., and Shaw, A. S. (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine Cell 84, 889-897
6. van Heusden, G. P. (2009) 14-3-3 proteins: insights from genome-wide studies in yeast Genomics 94, 287-293
7. Truong, A. B., Masters, S. C., Yang, H., and Fu, H. (2002) Role of the 14-3-3 C-terminal loop in ligand interaction Proteins 49, 321-325 (Pubitemid 35231467)
8. Obsilova, V., Herman, P., Vecer, J., Sulc, M., Teisinger, J., and Obsil, T. (2004) 14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232 J. Biol. Chem. 279, 4531-4540 (Pubitemid 38199044)
9. Silhan, J., Obsilova, V., Vecer, J., Herman, P., Sulc, M., Teisinger, J., and Obsil, T. (2004) 14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding J. Biol. Chem. 279, 49113-49119 (Pubitemid 39625794)
10. Shen, W., Clark, A. C., and Huber, S. C. (2003) The C-terminal tail of Arabidopsis 14-3-3omega functions as an autoinhibitor and may contain a tenth alpha-helix Plant J. 34, 473-484 (Pubitemid 36631878)
11. van Heusden, G. P. and Yde Steensma, H. (2006) Yeast 14-3-3 proteins Yeast 23, 159-171
12. Ross, C. A., Poirier, M. A., Wanker, E. E., and Amzel, M. (2003) Polyglutamine fibrillogenesis: the pathway unfolds Proc. Natl. Acad. Sci. U.S.A. 100, 1-3 (Pubitemid 36078018)
13. Obsil, T., Ghirlando, R., Klein, D. C., Ganguly, S., and Dyda, F. (2001) Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation Cell 105, 257-267 (Pubitemid 32429515)
14. Obsilova, V., Vecer, J., Herman, P., Pabianova, A., Sulc, M., Teisinger, J., Boura, E., and Obsil, T. (2005) 14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4 Biochemistry 44, 11608-11617 (Pubitemid 41209097)
15. Houtman, J. C., Brown, P. H., Bowden, B., Yamaguchi, H., Appella, E., Samelson, L. E., and Schuck, P. (2007) Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling Protein Sci. 16, 30-42 (Pubitemid 46036496)
16. Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78, 1606-1619 (Pubitemid 30141584)
17. Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2 nd ed., Kluwer Academic/Plenum Publishers, New York.
18. Lacourciere, K. A., Stivers, J. T., and Marino, J. P. (2000) Mechanism of neomycin and Rev peptide binding to the Rev responsive element of HIV-1 as determined by fluorescence and NMR spectroscopy Biochemistry 39, 5630-5641
19. Bryan, R. K. (1990) Maximum-entropy analysis of oversampled data problems Eur. Biophys. J. 18, 165-174
20. Vecer, J. and Herman, P. (2010) Maximum entropy analysis of analytically simulated complex fluorescence decays, J. Fluoresc. (DOI 10.1007/s10895-009- 0589-1).
21. Lavalette, D., Tetreau, C., Tourbez, M., and Blouquit, Y. (1999) Microscopic viscosity and rotational diffusion of proteins in a macromolecular environment Biophys. J. 76, 2744-2751 (Pubitemid 29264634)
22. Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H., Gamblin, S. J., Smerdon, S. J., and Cantley, L. C. (1997) The structural basis for 14-3-3:phosphopeptide binding specificity Cell 91, 961-971 (Pubitemid 28027829)
23. Murphy, L. R., Matubayasi, N., Payne, V. A., and Levy, R. M. (1998) Protein hydration and unfolding - insights from experimental partial specific volumes and unfolded protein models Folding Des. 3, 105-118 (Pubitemid 28166182)
24. Rittinger, K., Budman, J., Xu, J., Volinia, S., Cantley, L. C., Smerdon, S. J., Gamblin, S. J., and Yaffe, M. B. (1999) Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding Mol. Cell 4, 153-166 (Pubitemid 29456884)
25. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G., and Thompson, J. D. (2003) Multiple sequence alignment with the Clustal series of programs Nucleic Acids Res. 31, 3497-3500 (Pubitemid 37442184)