Literature DB >> 9129338

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

K Debel1, W D Sierralta, H P Braun, U K Schmitz, K Kloppstech.   

Abstract

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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Year:  1997        PMID: 9129338     DOI: 10.1007/s004250050074

Source DB:  PubMed          Journal:  Planta        ISSN: 0032-0935            Impact factor:   4.116


  23 in total

1.  Synthesis of the early light-inducible protein is controlled by blue light and related to light stress.

Authors:  I Adamska; I Ohad; K Kloppstech
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205

2.  A Low Molecular Mass Heat-Shock Protein Is Localized to Higher Plant Mitochondria.

Authors:  C. Lenne; R. Douce
Journal:  Plant Physiol       Date:  1994-08       Impact factor: 8.340

3.  Heat shock and other stress response systems of plants.

Authors:  D Neumann; L Nover; B Parthier; R Rieger; K D Scharf; R Wollgiehn; U zur Nieden
Journal:  Results Probl Cell Differ       Date:  1989

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Authors:  W M Bonner; R A Laskey
Journal:  Eur J Biochem       Date:  1974-07-01

5.  A low-viscosity epoxy resin embedding medium for electron microscopy.

Authors:  A R Spurr
Journal:  J Ultrastruct Res       Date:  1969-01

6.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

7.  Sequence and expression of the mRNA encoding HSP22, the mitochondrial small heat-shock protein in pea leaves.

Authors:  C Lenne; M A Block; J Garin; R Douce
Journal:  Biochem J       Date:  1995-11-01       Impact factor: 3.857

8.  Small heat shock proteins are molecular chaperones.

Authors:  U Jakob; M Gaestel; K Engel; J Buchner
Journal:  J Biol Chem       Date:  1993-01-25       Impact factor: 5.157

9.  Proteins Associated with Adaptation of Cultured Tobacco Cells to NaCl.

Authors:  N K Singh; A K Handa; P M Hasegawa; R A Bressan
Journal:  Plant Physiol       Date:  1985-09       Impact factor: 8.340

10.  Intracellular localization of heat shock proteins in maize.

Authors:  P Cooper; T H Ho
Journal:  Plant Physiol       Date:  1987-08       Impact factor: 8.340

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  1 in total

1.  The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress.

Authors:  S A Heckathorn; C A Downs; T D Sharkey; J S Coleman
Journal:  Plant Physiol       Date:  1998-01       Impact factor: 8.340

  1 in total

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