Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism

Biochemical and Biophysical Research Communications

Volumn 349, Issue 1, 2006, Pages 167-171

  Fu, Xinmiao ^a,b   Chang, Zengyi ^a,b  

^a PEKING UNIVERSITY   (China)

^b TSINGHUA UNIVERSITY   (China)

Author keywords

bis ANS; Chaperone; Hsp16.3; N terminal region; Small heat shock protein

Indexed keywords

1,1' BI(4 ANILINO)NAPHTHALENE 5,5' DISULFONIC ACID; ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 16.3; NAPHTHALENESULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; DISSOCIATION; HYDROPHOBICITY; MASS SPECTROMETRY; MOLECULAR RECOGNITION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN STABILITY; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

ALPHA-CRYSTALLINS; AMINO ACID SEQUENCE; ANILINO NAPHTHALENESULFONATES; BACTERIAL PROTEINS; BINDING SITES; CHAPERONINS; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

MYCOBACTERIUM TUBERCULOSIS;

EID: 33748296234     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.08.036     Document Type: Article

References (27)

1. Buchner J., Ehrnsperger M., Gaestel M., and Walke S. Purification and characterization of small heat shock proteins. Methods Enzymol. 290 (1998) 339-349
2. Kappe G., Leunissen J.A., and de Jong W.W. Evolution and diversity of prokaryotic small heat shock proteins. Prog. Mol. Subcell. Biol. 28 (2000) 1-17
3. Arrigo A.P., and Landry J. Expression and function of the low-molecular-weight heat-shock proteins. In: Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds). The Biology of Heat Shock Proteins and Molecular Chaperones (1994), Cold Spring Harbor Laboratory Press, New York 335-374
4. Plesofsky-Vig N., Vig J., and Brambl R. Phylogeny of the alpha-crystallin-related heat-shock proteins. J. Mol. Evol. 35 (1992) 537-545
5. Waters E.R., Lee G., and Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47 (1996) 325-338
6. Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H.E., Chen S., Raibil H.R., and Buchner J. Hsp26: a temperature-regulated chaperone. EMBO J. 18 (1999) 6744-6751
7. Kim K.K., Kim R., and Kim S.H. Crystal structure of a small heat-shock protein. Nature 394 (1998) 595-599
8. Fu X., and Chang Z. Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun. 316 (2004) 291-299
9. Fu X., Zhang H., Zhang X., Cao Y., Jiao W., Liu C., Song Y., Abulimiti A., and Chang Z. A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins. J. Biol. Chem. 280 (2005) 6337-6348
10. Gu L., Abulimiti A., Li W., and Chang Z. Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J. Mol. Biol. 319 (2002) 517-526
11. Sharma K.K., Kaur H., and Kester K. Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha-crystallin. Biochem. Biophys. Res. Commun. 239 (1997) 217-222
12. Sharma K.K., Kumar G.S., Murphy A.S., and Kester K. Identification of 1,1-Bi(4-anilino)naphthalene-5,5-disulfonic acid binding sequences in alpha-crystallin. J. Biol. Chem. 273 (1998) 15474-15478
13. Chang Z., Primm T.P., Jakana J., Lee I.H., Serysheva I., Chiu W., Gilbert H.F., and Quiocho F.A. Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 271 (1996) 7218-7224
14. Fu X., Liu C., Liu Y., Feng X., Gu L., Chen X., and Chang Z. Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation. Biochem. Biophys. Res. Commun. 310 (2003) 412-420
15. Kennaway C.K., et al. Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. J. Biol. Chem. 280 39 (2005) 33419-33425
16. Sharma K.K., Kaur H., Kumar G.S., and Kester K. Interaction of 1,1′-Bi(4-anilino)naphthalene-5,5′-disulfonic acid with alpha-crystallin. J. Biol. Chem. 273 (1998) 8965-8970
17. Lee G.J., Roseman A.M., Saibil H.R., and Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16 (1997) 659-671
18. Fu X., Li W., Mao Q., and Chang Z. Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones. Biochem. Biophys. Res. Commun. 308 (2003) 627-635
19. Fu X., and Chang Z. Identification of a highly conserved pro-gly doublet in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3. Biochemistry (Mosc) 71 Suppl. 1 (2006) S83-S90
20. Chen X. Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structures. Biochemistry (Mosc) 70 8 (2005) 913-919
21. Das K.P., and Surewicz W.K. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369 (1995) 321-325
22. Das K.P., and Surewicz W.K. On the substrate specificity of alpha-crystallin as a molecular chaperone. Biochem. J. 311 (1995) 367-370
23. Fu X., Jiao W., and Chang Z. Phylogenetic and biochemical studies reveal a potential evolutionary origin of small heat shock proteins of animals from bacterial class A. J. Mol. Evol. 62 (2006) 257-266
24. van Montfort R.L.M., Basha E., Fieldrich K.L., and Viering E. Crystal structure and assembly of a eukaryotic small heat shock protein. Nature Struct. Biol. 8 (2001) 1025-1030
25. Rao C.M., Raman B., Ramakrishna T., Rajaraman K., Ghosh D., Datta S., Trivedi V.D., and Sukhaswami M.B. Structural perturbation of a-crystallin and its chaperone-like activity. Int. J. Biol. Macromol. 22 (1998) 271-281
26. Friedrich K.L., et al. Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J. Biol. Chem. 279 2 (2004) 1080-1089
27. Sharma K.K., Kumar R.S., Kumar G.S., and Quinn P.T. Synthesis and characterization of a peptide identified as a functional element in alpha-crystallin. J. Biol. Chem. 275 (2000) 3767-3771