The major low-molecular-weight heat shock protein in chloroplasts shows antigenic conservation among diverse higher plant species.

E. Vierling, L. M. Harris, Qiang Chen

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Abstract

Several plant species are known to synthesize low-molecular-weight nucleus-encoded heat shock proteins (HSPs) which localize to chloroplasts. DNA sequence analysis of chloroplast HSP cDNAs from pea (Pisum sativum) and soybean (Glycine max) has shown that the carboxyl-terminal halves of these proteins are homologous to low-molecular-weight HSPs from a wide range of eucaryotes (E. Vierling, R. T. Nagao, A. E. DeRocher, and L. M. Harris, EMBO J. 7:575-581, 1988). We used a pea cDNA to construct fusion proteins containing either the carboxyl-terminal heat shock domain or the amino-terminal domain of the chloroplast HSP. The fusion proteins were overexpressed in Escherichia coli and used to produce choloroplast HSP-specific polyclonal antibodies. The carboxyl-terminal antibodies recognized chloroplast HSP precursor proteins from pea and from three divergent plant species, Arabidopsis thaliana, petunia (Petunia hybrida), and maize (Zea mays). The amino-terminal antibodies recognized effectively only the pea precursor. When intact plants of each species were subjected to a heat stress regime mimicking field growth conditions, significant levels of the mature forms of the chloroplast HSPs accumulated in pea, A. thaliana, and maize. The levels of accumulated HSPs remained unchanged for 12 h following the stress treatment. We conclude that the synthesis of chloroplast-localized HSPs is an important component of the stree response in all higher plants and that chloroplast HSPs from dicotyledonous and monocotyledonous plants have a conserved carboxyl-terminal domain.

Original languageEnglish (US)
Pages (from-to)461-468
Number of pages8
JournalMolecular and Cellular Biology
Volume9
Issue number2
StatePublished - Feb 1989

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Chloroplasts
Heat-Shock Proteins
Molecular Weight
Chloroplast Proteins
Peas
Petunia
Zea mays
Soybeans
Arabidopsis
Antibodies
Proteins
Complementary DNA
Hot Temperature
Protein Precursors
DNA Sequence Analysis
Shock
Escherichia coli

ASJC Scopus subject areas

  • Cell Biology
  • Genetics
  • Molecular Biology

Cite this

The major low-molecular-weight heat shock protein in chloroplasts shows antigenic conservation among diverse higher plant species. / Vierling, E.; Harris, L. M.; Chen, Qiang.

In: Molecular and Cellular Biology, Vol. 9, No. 2, 02.1989, p. 461-468.

Research output: Contribution to journalArticle

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