Comparison of the Structure and Expression Pattern for a Low Molecular Weight Heat-Shock Protein cDNa Clone from Nicotiana tabacum

Molecules and Cells

Volumn 8, Issue 5, 1998, Pages 594-599

  Park, Soo Min ^a   Bong, Choo Bong ^a  

^a Seoul National University   (South Korea)

Author keywords

cDNA Clone; Common Cultivars; LMW Heat Shock Protein; Nicotiana fabacum; Sequence Comparison

Indexed keywords

COMPLEMENTARY DNA; HEAT SHOCK PROTEIN; PLANT DNA; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; DNA SEQUENCE; GENE EXPRESSION REGULATION; GENETICS; GENOME; MOLECULAR CLONING; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PLANT; SEQUENCE HOMOLOGY; SOUTHERN BLOTTING; SPECIES DIFFERENCE; TOBACCO;

AMINO ACID SEQUENCE; BASE SEQUENCE; BLOTTING, SOUTHERN; CLONING, MOLECULAR; DNA, COMPLEMENTARY; DNA, PLANT; GENE EXPRESSION REGULATION, PLANT; GENOME, PLANT; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OPEN READING FRAMES; PLANT PROTEINS; PLANTS, TOXIC; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; TOBACCO;

EID: 0032585101     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (31)

1. Bartling, D., Bulter, H., Liebeton, K., and Weiler, E. W. (1992) An Arabidopsis thaliana cDNA clone encoding a 17.6 kDa class II heat shock protein. Plant Mol. Biol. 18, 1009-1008.
2. Caspers, G. -J., Leunissen, J. A. M., and De Jong, W. W. (1995) The expanding small heat shock protein family, and structure predictions of the conserved 'a-crystallin domain'. J. Mol. Evol. 40, 238-248.
3. Darwish, K., Wang, L. Q., Hwang, C. H., Apuya, N., and Zimmerman, J. L. (1991) Cloning and characterization of genes encoding low molecular weight heat shock proteins from carrot. Plant Mol. Biol. 16, 729-731.
4. Ehrnsperger, M., Simone G., Matthias G., and Johannes B. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229.
5. Gyorgyey, J., Gartner, A., nemeth, K., Hirt, H., Heberle-Bors, E., and Dudits, D. (1991) Alfalfa heat shock genes are differentially expressed during somatic embryogenesis. Plant Mol. Biol. 16, 999-1007.
6. Hartl, F. U., Hlodan, R., and Langer, T. (1994) Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19, 20-25.
7. Heckathorn, S. A., Downs, C. A., Sharkey, T. D., and Coleman, J. S. (1998) The small, methionine-rich chloroplast heat-shock proteins protects photosystem II electron transport during heat stress. Plant Physiol. 116, 439-444.
8. Jorgensen, J. A. and Nguyen, H. T. (1995) Genetic analysis of heat shock proteins in maize. Theor. Appl. Genet. 91, 38-46.
9. Joshi, C. P. and Nguyen, H. T. (1996) Differential display-mediated rapid identification of different members of a multigene family, HSP 16.9 in wheat. Plant Mol Biol. 31, 575-584.
10. Junghans, H. and Metzlaf, M. (1990) A simple and rapid method for the preparation of total plant DNA. Biotechniques 8, 176.
11. Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol 157, 105-132.
12. LaFayette, P. R., Nagao, R. T., O'Grady, K., Vierling, E., and Key, J. L. (1996) Molecular characterization of cDNAs encoding low-molecular-weight heat shock proteins of soybean. Plant Mol. Biol. 30, 159-169.
13. Lauzon, L. M., Helm, K. W., and Vierling, E. (1990) A cDNA clone from Pisum sativum encoding a low molecular weight heat shock protein. Nucleic Acids Res. 18, 4274.
14. Lawrence, S. D., Cline, K., and Moore, G. A. (1997) Chromoplast development in ripening tomato fruit: identification of cDNAs for chromoplast-targeted proteins and characterization of a cDNA encoding a plast-localized low-molecular-weight heat shock protein. Plant Mol. Biol. 33. 483-492.
15. Lee, G. J., Roseman, A. M., Saibil, H. R., and Vierling, E. (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16, 659-671.
16. Leroux, M. R., Melki, R., Gordon, B., Batelier, G., and Candido, E. P. M. (1997) Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272, 24646-24656.
17. Mansfield, M. A. and Key, J. L. (1987) Synthesis of the low molecular weight heat shock proteins in plants. Plant Physiol. 84, 1007-1017.
18. Mehlen, R, Hickey, E., Weber, L. A., and Arrigo, A.-P. (1997) Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFa in NIH-3T3-ras cells. Biochem. Biophys. Res. Commun. 241, 187-192.
19. Melville, M. W., Hansen, W. J., Freeman, B. C., Welch, W. J., and Katze, M. G. (1997) The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR. Proc. Natl. Acad. Sci. USA 94, 97-102.
20. Miernyk, J. A. and Hayman, T. G. (1996) ATPase activity and molecular chaperone function of the stress70 proteins. Plant Physiol. 110, 419-424.
21. Muchowski, P. J., Bassuk, J. A., Lubsen, N. H., and Clark, J. I. (1997) Human alphaB-crystallin; Small heat shock protein and molecular chaperone. J. Biol. Chem. 272, 2578-2582.
22. Park, S. M., Cho, H. S., Song, H. W., Shu, J. W., and Hong, C. B. (1994) Nicotiana tabacum low molecular weight heat shock protein cDNA clones and their expression patterns. Mol. Cells 4, 393-397.
23. Park. S.-Y., Shivaji, R., Krans, J. V., and Luthe, D. S. (1996) Heat-shock response in heat-tolerant and nontolerant variants of Agrostis palustris Huds. Plant Physiol. 111, 515-524.
24. Parsell, D. A. and Lindquist, S. (1993) The function of heat-shock proteins in stress tolerance: degradation ana reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
25. Ritossa, F. (1962) A new puffing pattern induced by heat shock and DNP in Drosophila. Experientia 18, 571-573.
26. Rothnie, H. M., Jacqueline R., and Thomas H. (1994) The contribution of AAUAAA and the upstream element UUUGUA to the efficiency of mRNA 3′-end formation in plants. EMBO J. 13, 2200-2210.
27. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
28. Tzeng, S.-S., Yeh, K. W., Chen, Y. M., and Lin, C.-Y. (1992) Two Oryza saliva genomic DNA clones 16.9-kDa heat shock proteins. Plant Physiol. 99, 1723-1725.
29. Waters, Elizabeth R. (1995) The molecular evolution of the small heat-shock proteins in plants. Genetics 141, 785-795.
30. Waters, E. R., Garrett J.-L., and Elizabeth V. (1996) Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47, 325-338.
31. Wu, D. H. and Laidman, D. L. (1996) Isolation of six low molecular weight heat shock proteins and partial characterization of heat shock protein 29 from mung bean hypocotyl. Phytochemistry 44, 985-989.