Accumulation of plastid HSP 23 of <i>Chenopodium rubrum</i> is controlled post‐translationally by light

Debel, Karsten; Knack, Gaby; Kloppstech, Klaus

doi:10.1046/j.1365-313x.1994.6010079.x

Cited by 10 publications

(12 citation statements)

References 16 publications

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“…Lanes: 1, soluble proteins; 2, membrane-bound proteins; 3, protein extract of isolated intact chloroplasts; 4, stromal proteins of isolated intact chloroplasts; 5, membrane-bound proteins of isolated intact chloroplasts; 6, protein extract of washed mitochondria; 7, soluble proteins of washed mitochondria; 8, membrane-bound proteins of washed mitochondria (data not shown). There was no reaction of the antibody with proteins of non-heat-shocked cells, as demonstrated earlier (Debel et al 1994). These data can only be taken as a first hint of the mitochondrial localization of HSP23, as the protein separations from these organelles are contaminated with other cellular components.…”

Section: Resultssupporting

confidence: 74%

“…After posttranslational transport of the precursor into isolated pea chloroplasts we obtained a processed and protease-resistant protein band of the correct size, and we reasoned that this HSP should be localized within the chloroplast . We interpreted the observation that the amount of accumulated protein is influenced by the light intensity during heat shock (Debel et al 1994) as additional evidence for a chloroplastic location as we expected that light stress would primarily affect the chloroplast. This interpretation seemed plausible in spite of the fact that the amino acid sequence of HSP23 showed only a low similarity to known small plastid HSPs (Vierling 1991).…”

Section: Introductionmentioning

confidence: 99%

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The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria

Debel

Sierralta²,

Braun

et al. 1997

Planta

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The 23-kDa nuclear-encoded heat-shock protein (HSP) of Chenopodium rubrum L. is regulated by light at the posttranslational level. Higher light intensities are more effective in inducing the accumulation of the mature protein under heat-shock conditions. Based on this and other properties the protein was considered to belong to the group of small chloroplastic HSPs. However, we have now obtained the following evidence that this 23-kDa HSP is localized in the mitochondria: (i) Immunogold-labelled protein was almost exclusively restricted to the mitochondria in electron microscope thin sections. (ii) Using purified, isolated mitochondria from potato tubers the in-vitro-synthesized translation product of 31 kDa was readily transported into mitochondria where it was processed to the 23-kDa product. (iii) The protein could be detected by Western blotting in a preparation of washed mitochondria of Chenopodium, while under the same conditions no signal could be obtained in a preparation of isolated chloroplasts. (iv) Finally, sequence comparison with the published sequences of mitochondrial proteins by Lenne et al. (1995, Biochem J 311:805-813) and LaFayette et al. (1996, Plant Mol Biol 30:159-169) showed clearly that the 23-kDa protein is considerably more similar to these two proteins than to the group of plastid small HSPs. From these data we infer that mitochondria are involved in the response of the plants to high light stress under heat-shock conditions.

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Section: Resultssupporting

confidence: 74%

Section: Introductionmentioning

confidence: 99%

The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria

Debel

Sierralta²,

Braun

et al. 1997

Planta

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“…Other light-stress proteins are identical to the small heat-shock proteins of Chenopodium and barley (Debel et al 1994). Interestingly, both the Chenopodium protein which has now been localized in the mitochondrion (K. Debel, our Institute, personal communication) -and which may be related to the protein recently described by Lenne and Douce (1994) -and the small chloroplastic heat-shock protein of barley are regulated in a very similar manner, again indicating the complex interrelationship between different organelles during light stress and photorespiration.…”

Section: Discussionmentioning

confidence: 99%

The expression of mRNAs for light-stress proteins in barley: Inverse relationship of mRNA levels of individual genes within the leaf gradient

Pötter

Beator

Kloppstech

1996

Planta

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Two cDNAs coding for putative light-stress proteins of barley (Hordeum vulgare L.) were cloned and the expression of the corresponding mRNAs analyzed in the barley leaf and compared to that of the well-studied ELIP (early-inducible protein) mRNA. During greening the mRNA for clone HL No. 2, which shows homology to two rice proteins of as yet unknown function, was transiently induced; its level rose more slowly and remained elevated for a longer time than was described for ELIP mRNAs. The mRNA corresponding to clone HL No. 13 was recognized as homologous to subunit P of pea glycine decarboxylase, a nuclear-encoded mitochondrial protein involved in photorespiration. Its mRNA level rose more slowly with cellular development than that of the mRNA for LHC II, the apoprotein of the chlorophyll-a/b-binding protein of PSII. The mRNAs of both novel proteins were induced by high light up to an irradiance of 2000 W.m-2. Their levels remained elevated under high light for up to 9 h, the longest time span examined, while after return to culture light conditions the mRNAs rapidly decayed, each with an individual time course. In green barley leaves the mRNA for clone HL No. 2 was expressed to the highest level in the most basal segment, similar to that of ELIPs, while in contrast the mRNA for subunit P of glycine decarboxylase accumulated to the highest level in the leaf apex where the fully developed cells and mitochondria reside. The latter finding strongly indicates that photorespiration is regulated by high light also at the level of mRNA transcription or mRNA accumulation. In addition, we show that perception of light stress is under the control of cellular development and differentiation.

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“…However, the authors did not examine whether under these conditions high light protected the leaves from irreversible heat damage. According to Debel et al (1994), high light caused post-translational accumulation of plastid HSP 23 in heat-stressed cell cultures of Chenopodium rubrum L. In leaves of Solidago altissima L., HSP synthesis, particularly formation of HSP 70 and small HSPs, was found to be enhanced by the combined action of heat and high light (Barua and Heckathorn 2006). In Arabidopsis thaliana (L.) Heynh, Rossel et al (2002) observed enforced gene expression by high light for several HSPs and other chaperones, including a chloroplasttargeted putative small HSP.…”

Section: Discussionmentioning

confidence: 99%

Light-stimulated heat tolerance in leaves of two neotropical tree species, Ficus insipida and Calophyllum longifolium

Krause

Winter

Krause

et al. 2015

Functional Plant Biol.

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Abstract. Previous heat tolerance tests of higher plants have been mostly performed with darkened leaves. However, under natural conditions, high leaf temperatures usually occur during periods of high solar radiation. In this study, we demonstrate small but significant increases in the heat tolerance of illuminated leaves. Leaf disks of mature sun leaves from two neotropical tree species, Ficus insipida Willd. and Calophyllum longifolium Willd., were subjected to 15 min of heat treatment in the light (500 mmol photons m -2 s -1 ) and in the dark. Tissue temperatures were controlled by floating the disks on the surface of a water bath. PSII activity was determined 24 h and 48 h after heating using chlorophyll a fluorescence. Permanent tissue damage was assessed visually during long-term storage of leaf sections under dim light. In comparison to heat treatments in the dark, the critical temperature (T 50 ) causing a 50% decline of the fluorescence ratio F v /F m was increased by~1 C (from~52.5 C to~53.5 C) in the light. Moreover, illumination reduced the decline of F v /F m as temperatures approached T 50 . Visible tissue damage was reduced following heat treatment in the light. Experiments with attached leaves of seedlings exposed to increasing temperatures in a gas exchange cuvette also showed a positive effect of light on heat tolerance.

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Accumulation of plastid HSP 23 of Chenopodium rubrum is controlled post‐translationally by light

Cited by 10 publications

References 16 publications

The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria

The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria

The expression of mRNAs for light-stress proteins in barley: Inverse relationship of mRNA levels of individual genes within the leaf gradient

Light-stimulated heat tolerance in leaves of two neotropical tree species, Ficus insipida and Calophyllum longifolium

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