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Plant Physiology logoLink to Plant Physiology
. 1996 Jan;110(1):241–248. doi: 10.1104/pp.110.1.241

Induction and Regulation of Heat-Shock Gene Expression by an Amino Acid Analog in Soybean Seedlings.

YRJ Lee 1, R T Nagao 1, C Y Lin 1, J L Key 1
PMCID: PMC157715  PMID: 12226180

Abstract

The effect of the proline analog azetidine-2-carboxylic acid (Aze) on the induction and the regulation of heat-shock (HS) mRNA accumulation and heat-shock protein (HSP) synthesis in soybean (Glycine max) seedlings was studied. Treatment with Aze elicited an HS-like response at the normal growth temperature, 28[deg]C, with seven of nine HS cDNA clones tested. Two cDNA clones, Gm-Hsp22.5 and pFS2033, share 78% identity; however, transcripts hybridizing to GmHsp22.5 but not pFS2033 accumulated with Aze treatment at 28[deg]C. Substantial incorporation of radioactive amino acid into high molecular weight HSPs but not low molecular weight HSPs was observed in vivo during Aze treatment at 28[deg]C. Low molecular weight HSPs were detected using antibodies raised against an abundant member of low molecular weight class I HSPs, indicating that low molecular weight HSPs were synthesized at normal growth temperatures during Aze treatment despite a lack of substantial in vivo radioactive amino acid incorporation. In summary, Aze treatment induced accumulation of most but not all HS mRNAs and HSPs in soybean seedlings; the observations presented here suggest differential regulation among various HS genes at the transcriptional and posttranscriptional levels.

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Selected References

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  1. Ananthan J., Goldberg A. L., Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science. 1986 Apr 25;232(4749):522–524. doi: 10.1126/science.3083508. [DOI] [PubMed] [Google Scholar]
  2. DiDomenico B. J., Bugaisky G. E., Lindquist S. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell. 1982 Dec;31(3 Pt 2):593–603. doi: 10.1016/0092-8674(82)90315-4. [DOI] [PubMed] [Google Scholar]
  3. Droog F. N., Hooykaas P. J., Libbenga K. R., van der Zaal E. J. Proteins encoded by an auxin-regulated gene family of tobacco share limited but significant homology with glutathione S-transferases and one member indeed shows in vitro GST activity. Plant Mol Biol. 1993 Mar;21(6):965–972. doi: 10.1007/BF00023595. [DOI] [PubMed] [Google Scholar]
  4. Edelman L., Czarnecka E., Key J. L. Induction and Accumulation of Heat Shock-Specific Poly(A) RNAs and Proteins in Soybean Seedlings during Arsenite and Cadmium Treatments. Plant Physiol. 1988 Apr;86(4):1048–1056. doi: 10.1104/pp.86.4.1048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Edington B. V., Whelan S. A., Hightower L. E. Inhibition of heat shock (stress) protein induction by deuterium oxide and glycerol: additional support for the abnormal protein hypothesis of induction. J Cell Physiol. 1989 May;139(2):219–228. doi: 10.1002/jcp.1041390202. [DOI] [PubMed] [Google Scholar]
  6. Goff S. A., Goldberg A. L. Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes. Cell. 1985 Jun;41(2):587–595. doi: 10.1016/s0092-8674(85)80031-3. [DOI] [PubMed] [Google Scholar]
  7. Gurley W. B., Key J. L. Transcriptional regulation of the heat-shock response: a plant perspective. Biochemistry. 1991 Jan 8;30(1):1–12. doi: 10.1021/bi00215a001. [DOI] [PubMed] [Google Scholar]
  8. Helm K. W., LaFayette P. R., Nagao R. T., Key J. L., Vierling E. Localization of small heat shock proteins to the higher plant endomembrane system. Mol Cell Biol. 1993 Jan;13(1):238–247. doi: 10.1128/mcb.13.1.238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hightower L. E. Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides. J Cell Physiol. 1980 Mar;102(3):407–427. doi: 10.1002/jcp.1041020315. [DOI] [PubMed] [Google Scholar]
  10. Hsieh M. H., Chen J. T., Jinn T. L., Chen Y. M., Lin C. Y. A class of soybean low molecular weight heat shock proteins : immunological study and quantitation. Plant Physiol. 1992 Aug;99(4):1279–1284. doi: 10.1104/pp.99.4.1279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jones K. A., Findly R. C. Induction of heat shock proteins by canavanine in Tetrahymena. No change in ATP levels measured in vivo by NMR. J Biol Chem. 1986 Jul 5;261(19):8703–8707. [PubMed] [Google Scholar]
  12. Kelley P. M., Schlesinger M. J. The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts. Cell. 1978 Dec;15(4):1277–1286. doi: 10.1016/0092-8674(78)90053-3. [DOI] [PubMed] [Google Scholar]
  13. Key J. L., Lin C. Y., Chen Y. M. Heat shock proteins of higher plants. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3526–3530. doi: 10.1073/pnas.78.6.3526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Knecht D. A., Dimond R. L. Visualization of antigenic proteins on Western blots. Anal Biochem. 1984 Jan;136(1):180–184. doi: 10.1016/0003-2697(84)90321-x. [DOI] [PubMed] [Google Scholar]
  15. Lin C. Y., Roberts J. K., Key J. L. Acquisition of Thermotolerance in Soybean Seedlings : Synthesis and Accumulation of Heat Shock Proteins and their Cellular Localization. Plant Physiol. 1984 Jan;74(1):152–160. doi: 10.1104/pp.74.1.152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mansfield M. A., Key J. L. Synthesis of the low molecular weight heat shock proteins in plants. Plant Physiol. 1987 Aug;84(4):1007–1017. doi: 10.1104/pp.84.4.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Nagao R. T., Kimpel J. A., Key J. L. Molecular and cellular biology of the heat-shock response. Adv Genet. 1990;28:235–274. doi: 10.1016/s0065-2660(08)60528-3. [DOI] [PubMed] [Google Scholar]
  18. Parsell D. A., Lindquist S. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet. 1993;27:437–496. doi: 10.1146/annurev.ge.27.120193.002253. [DOI] [PubMed] [Google Scholar]
  19. Roberts J. K., Key J. L. Isolation and characterization of a soybean hsp70 gene. Plant Mol Biol. 1991 Apr;16(4):671–683. doi: 10.1007/BF00023431. [DOI] [PubMed] [Google Scholar]
  20. Schöffl F., Key J. L. An analysis of mRNAs for a group of heat shock proteins of soybean using cloned cDNAs. J Mol Appl Genet. 1982;1(4):301–314. [PubMed] [Google Scholar]
  21. Stone D. E., Craig E. A. Self-regulation of 70-kilodalton heat shock proteins in Saccharomyces cerevisiae. Mol Cell Biol. 1990 Apr;10(4):1622–1632. doi: 10.1128/mcb.10.4.1622. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Straus D., Walter W., Gross C. A. DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev. 1990 Dec;4(12A):2202–2209. doi: 10.1101/gad.4.12a.2202. [DOI] [PubMed] [Google Scholar]
  23. Thomas G. P., Mathews M. B. Alterations of transcription and translation in HeLa cells exposed to amino acid analogs. Mol Cell Biol. 1984 Jun;4(6):1063–1072. doi: 10.1128/mcb.4.6.1063. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Vierling E., Mishkind M. L., Schmidt G. W., Key J. L. Specific heat shock proteins are transported into chloroplasts. Proc Natl Acad Sci U S A. 1986 Jan;83(2):361–365. doi: 10.1073/pnas.83.2.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Vierling E., Nagao R. T., DeRocher A. E., Harris L. M. A heat shock protein localized to chloroplasts is a member of a eukaryotic superfamily of heat shock proteins. EMBO J. 1988 Mar;7(3):575–581. doi: 10.1002/j.1460-2075.1988.tb02849.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. White C. N., Hightower L. E. Stress mRNA metabolism in canavanine-treated chicken embryo cells. Mol Cell Biol. 1984 Aug;4(8):1534–1541. doi: 10.1128/mcb.4.8.1534. [DOI] [PMC free article] [PubMed] [Google Scholar]

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