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Jinn TL, Chang P, Chen YM, et al. Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean. Plant Physiol. 1997;114(2):429-438doi: 10.1104/pp.114.2.429.
Jinn, T. L., Chang, P., Chen, Y. M., Key, J. L., & Lin, C. Y. (1997). Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean. Plant physiology, 114(2), 429-438. https://doi.org/10.1104/pp.114.2.429
Jinn, T. L., et al. "Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean." Plant physiology vol. 114,2 (1997): 429-438. doi: https://doi.org/10.1104/pp.114.2.429
Jinn TL, Chang P, Chen YM, Key JL, Lin CY. Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean. Plant Physiol. 1997 Jun;114(2):429-438. doi: 10.1104/pp.114.2.429. PMID: 12223717; PMCID: PMC158322.
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Plant Physiol. 1997 Jun;114(2):429-438. doi: 10.1104/pp.114.2.429.

Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean.

Plant physiology

T. L. Jinn, PFL. Chang, Y. M. Chen, J. L. Key, C. Y. Lin

Affiliations

  1. Department of Botany, National Taiwan University, Taipei 106, Taiwan, Republic of China (T.-L.J., P.-F.L.C., Y.-M.C., C.-Y.L.).

PMID: 12223717 PMCID: PMC158322 DOI: 10.1104/pp.114.2.429

Abstract

A monospecific polyclonal antibody was used to study the tissue-type specificity and intracellular localization of class I low-molecular-weight (LMW) heat-shock proteins (HSPs) in soybean (Glycine max) under different heat-shock regimes. In etiolated soybean seedlings, the root meristematic regions contained the highest levels of LMW HSP. No tissue-type-specific expression of class I LMW HSP was detected using the tissue-printing method. In immunolocalization studies of seedlings treated with HS (40[deg]C for 2 h) the class I LMW HSPs were found in the aggregated granular structures, which were distributed randomly in the cytoplasm and in the nucleus. When the heat shock was released, the granular structures disappeared and the class I LMW HSPs became distributed homogeneously in the cytoplasm. When the seedlings were then given a more severe heat shock following the initial 40[deg]C -> 28[deg]C treatment, a large proportion of the class I LMW HSPs that originally localized in the cytoplasm were translocated into the nucleus and nucleolus. Class I LMW HSPs may assist in the resolubilization of proteins denatured or aggregated by heat and may also participate in the restoration of organellar function after heat shock.

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