A natively unfolded βγ-crystallin domain from Hahella chejuensis

Biochemistry

Volumn 49, Issue 45, 2010, Pages 9746-9755

  Srivastava, Atul K ^a   Sharma, Yogendra ^b   Chary, Kandala V R ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROPERTIES; CELLULAR FUNCTION; CONFORMATIONAL CHANGE; CONFORMATIONAL SWITCHES; CRYSTALLIN; FREE STATE; MOLTEN GLOBULE; NMR STRUCTURES; STRESS RESPONSE; STRUCTURAL SIMILARITY; UNFOLDED PROTEINS; YERSINIA PESTIS;

BINDING ENERGY; PROTEINS;

CALCIUM;

BETA GAMMA CRYSTALLIN; CALCIUM ION; CRYSTALLIN; MAGNESIUM ION; PROTEIN S; UNCLASSIFIED DRUG;

ARTICLE; CALCIUM BINDING; CELLULAR STRESS RESPONSE; CONFORMATIONAL TRANSITION; HAHELLA; HAHELLA CHEJUENSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BINDING SITES; CALCIUM; CALORIMETRY; CAULOBACTER; CIRCULAR DICHROISM; CRYSTALLINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; YERSINIA PESTIS;

CAULOBACTER VIBRIOIDES; HAHELLA CHEJUENSIS; YERSINIA PESTIS;

EID: 78149446241     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101000m     Document Type: Article

References (40)

1. Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N. H., Slingsby, C., and Tardieu, A. (2004) Ageing and vision: Structure, stability and function of lens crystallins Prog. Biophys. Mol. Biol. 86, 407-485
2. Wistow, G. (1990) Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins J. Mol. Evol. 30, 140-145
3. Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, I., Turnell, B., and Wistow, G. (1981) The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II Nature 289, 771-777
4. Wistow, G., Turnell, B., Summers, L., Slingsby, C., Moss, D., Miller, L., Lindley, P., and Blundell, T. (1983) X-ray analysis of the eye lens protein γ-II crystallin at 1.9 Å resolution J. Mol. Biol. 170, 175-202
5. Aravind, P., Mishra, A., Suman, S. K., Jobby, M. K., Sankaranarayanan, R., and Sharma, Y. (2009) The βγ-crystallin superfamily contains a universal motif for binding calcium Biochemistry 48, 12180-12190
6. Wenk, M., Baumgartner, R., Holak, T. A., Huber, R., Jaenicke, R., and Mayr, E. M. (1999) The domains of protein S from Myxococcus xanthus: Structure, stability and interactions J. Mol. Biol. 286, 1533-1545
7. 2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype γ-crystallin fold in aqueous solution J. Mol. Biol. 271, 645-655
8. Jaenicke, R. (1999) Stability and folding of domain proteins Prog. Biophys. Mol. Biol. 71, 155-241
9. Jaenicke, R. and Slingsby, C. (2001) Lens crystallins and their microbial homologs: Structure, stability, and function Crit. Rev. Biochem. Mol. Biol. 36, 435-499
10. Clout, N. J., Kretschmar, M., Jaenicke, R., and Slingsby, C. (2001) Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens βγ-crystallin domain fold Structure 9, 115-124
11. Rajini, B., Shridas, P., Sundari, C. S., Muralidhar, D., Chandani, S., Thomas, F., and Sharma, Y. (2001) Calcium binding properties of γ-crystallin: Calcium ion binds at the Greek key βγ-crystallin fold J. Biol. Chem. 276, 38464-38471
12. Wenk, M. and Mayr, E. M. (1998) Myxococcus xanthus spore coat protein S, a stress-induced member of the βγ-crystallin superfamily, gains stability from binding of calcium ions Eur. J. Biochem. 255, 604-610
13. Kretschmar, M., Mayr, E. M., and Jaenicke, R. (1999) Kinetic and thermodynamic stabilization of the βγ-crystallin homolog spherulin 3a from Physarum polycephalum by calcium binding J. Mol. Biol. 289, 701-705
14. Barnwal, R. P., Jobby, M. K., Devi, K. M., Sharma, Y., and Chary, K. V. (2009) Solution structure and calcium-binding properties of M-crystallin, a primordial βγ-crystallin from archaea J. Mol. Biol. 386, 675-689
15. Mukherjee, S., Kuchroo, K., and Chary, K. V. (2005) Structural characterization of the apo form of a calcium binding protein from Entamoeba histolytica by hydrogen exchange and its folding to the holo state Biochemistry 44, 11636-11645
16. Chin, D. and Means, A. R. (2000) Calmodulin: A prototypical calcium sensor Trends Cell Biol. 10, 322-328
17. Jeong, H., Yim, J. H., Lee, C., Choi, S. H., Park, Y. K., Yoon, S. H., Hur, C. G., Kang, H. Y., Kim, D., Lee, H. H., Park, K. H., Park, S. H., Park, H. S., Lee, H. K., Oh, T. K., and Kim, J. F. (2005) Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent Nucleic Acids Res. 33, 7066-7073
18. Srivastava, A. K., Sharma, Y., and Chary, K. V. (2008) Overexpression, on-column refolding and isotopic labeling of Hahellin from Hahella chejuensis, a putative member of the βγ-crystallin superfamily Protein Expression Purif. 58, 269-274
19. Jobby, M. K. and Sharma, Y. (2005) Calcium-binding crystallins from Yersinia pestis. Characterization of two single βγ-crystallin domains of a putative exported protein J. Biol. Chem. 280, 1209-1216
20. Jobby, M. K. and Sharma, Y. (2007) Caulollins from Caulobacter crescentus, a pair of partially unstructured proteins of βγ- crystallin superfamily, gain structure upon binding calcium Biochemistry 46, 12298-12307
21. Uversky, V. N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12
22. 1H NMR assignments of its pH-denatured state Proc. Natl. Acad. Sci. U.S.A. 91, 9412-9416
23. 15N resonance assignments of Hahellin from Hahella chejuensis, a putative member of the βγ- crystallin superfamily Biomol. NMR Assignments 2, 151-153
24. Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13, 289-302
25. Guntert, P. (2004) Automated NMR structure calculation with CYANA Methods Mol. Biol. 278, 353-378
26. Smith, L. J., Bolin, K. A., Schwalbe, H., MacArthur, M. W., Thornton, J. M., and Dobson, C. M. (1996) Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations J. Mol. Biol. 255, 494-506
27. Uversky, V. N. (2002) Natively unfolded proteins: A point where biology waits for physics Protein Sci. 11, 739-756
28. Jobby, M. K. and Sharma, Y. (2007) Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins FEBS J. 274, 4135-4147
29. Uversky, V. N., Li, J., and Fink, A. L. (2001) Evidence for a partially folded intermediate in α-synuclein fibril formation J. Biol. Chem. 276, 10737-10744
30. Uversky, V. N. (2003) Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go? Cell. Mol. Life Sci. 60, 1852-1871
31. Ptitsyn, O. B. (1995) Molten globule and protein folding Adv. Protein Chem. 47, 83-229
32. Tompa, P. (2002) Intrinsically unstructured proteins Trends Biochem. Sci. 27, 527-533
33. Lacy, E. R., Filippov, I., Lewis, W. S., Otieno, S., Xiao, L., Weiss, S., Hengst, L., and Kriwacki, R. W. (2004) p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding Nat. Struct. Mol. Biol. 11, 358-364
34. Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, I., Turnell, B., and Wistow, G. (1981) The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II Nature 289, 771-777
35. Mills, I. A., Flaugh, S. L., Kosinski-Collins, M. S., and King, J. A. (2007) Folding and stability of the isolated Greek key domains of the long-lived human lens proteins γD-crystallin and γS-crystallin Protein Sci. 16, 2427-2444
36. Hemmingsen, J. M., Gernert, K. M., Richardson, J. S., and Richardson, D. C. (1994) The tyrosine corner: A feature of most Greek key β-barrel proteins Protein Sci. 3, 1927-1937
37. Teintze, M., Inouye, M., and Inouye, S. (1988) Characterization of calcium-binding sites in development-specific protein S of Myxococcus xanthus using site-specific mutagenesis J. Biol. Chem. 263, 1199-1203
38. Villamil Giraldo, A. M., Lopez, M. M., Gonzalez, L. M., Pagano, R. S., Labriola, C. A., Landolfo, L., Delfino, J. M., Parodi, A. J., and Caramelo, J. J. (2010) The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration J. Biol. Chem. 285, 4544-4553
39. Del, C. N., Jeffery, E., Rizvi, S. M., Stamper, E., Peters, L. R., Brown, W. C., Provoda, C., and Raghavan, M. (2010) Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathway J. Biol. Chem. 285, 4520-4535
40. 2+ on the structure and hydroxyapatite binding properties of osteocalcin Biochim. Biophys. Acta 1535, 153-163