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

Debel, Karsten; Sierralta, Walter; Braun, Hans‐Peter; Schmitz, Udo K.; Kloppstech, Klaus

doi:10.1007/s004250050074

Cited by 14 publications

(6 citation statements)

References 32 publications

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“…Basic biochemical data from the analyses of the sHSPs with molecular masses ranging from 18 to 23.5 kDa (Fig. 3) corresponded with the data previously published for sHSP22 from Pisum sativum (Lenne et al 1995), sHSP22 from Zea mays (Lund et al 1998), sHSP23 from Chenopodium rubrum (Debel et al 1997) and sHSP23.5 from Arabidopsis thaliana (Visioli et al 1997). Seven of the eight characterized stress‐induced sHSPs exhibited acidic characteristics in agreement with previously published data on other sHSPs (Morrow et al 2000).…”

Section: Discussionsupporting

confidence: 84%

Identification of stress‐induced mitochondrial proteins in cultured tobacco cells

Hájek

Honys

Witters

et al. 2005

Physiologia Plantarum

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Under stress conditions, small and large heat-shock proteins cooperatively fulfil molecular chaperone activities within many cellular compartments, including mitochondria. Here, we report the identification and characterization of 10 newly synthesized low-molecular-weight heat stress-induced proteins (SIPs) found solely in the mitochondrial fraction of suspension-cultured cells of tobacco (Nicotiana tabacum L., strain Virginia Bright Italia-0). These SIPs were shown to be encoded by the nuclear genome and none was detected in non-stressed cells. Mass spectroscopy analysis revealed that eight SIPs belonged to the group of small heat-shock proteins, whilst one protein shared significant homology with transcription factors. De novo synthesis of all SIPs was detected within 10 min of the commencement of heat stress and continued for the whole 12 h stress interval. Moreover, nine of the SIPs were stable for 24 h following stress termination. SIP1, which showed the most intense synthesis profile, was found to be phosphorylated. The most intense stress response was observed mainly during the exponential growth phase of the cell culture. Native electrophoresis of mitochondrial protein complexes revealed an association of all the SIPs in high-molecular-weight complexes with no free SIPs left in mitochondria. These complexes were localized to the mitochondrial membrane fraction.Abbreviations -EST, expressed sequence tag; HSP, heat-shock protein; PMSF, phenylmethylsulphonyl fluoride; PVDF, polyvinylidene difluoride; sHSP, small heat-shock protein; SIP, stress-induced protein; VBI-0, Virginia Bright Italia-0.

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Section: Discussionsupporting

confidence: 84%

Identification of stress‐induced mitochondrial proteins in cultured tobacco cells

Hájek

Honys

Witters

et al. 2005

Physiologia Plantarum

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“…) and induced to combat misfolded and aggregated proteins (Debel et al. ; Dong et al. ; Driedonks et al.…”

Section: Discussionmentioning

confidence: 99%

Transcriptome Profiling of Bigelowiella natans in Response to Light Stress

Rangsrikitphoti

Durnford

2018

J Eukaryotic Microbiology

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Bigelowiella natans is a marine chlorarachniophyte whose plastid was acquired secondarily via endosymbiosis with a green alga. During plastid evolution, the photosynthetic endosymbiont would have integrated with the host metabolic pathways. This would require the evolution and coordination of strategies to cope with changes in light intensity that includes changes in the expression of both endosymbiont and host-derived genes. To investigate the transcriptional response to light intensity in chlorarachniophytes, we conducted an RNA-seq experiment to identify differentially expressed genes following a 4-h shift to high or very-low light. A shift to high light altered the expression of over 2,000 genes, many involved with photosynthesis, PSII assembly, primary metabolism, and reactive-oxygen scavenging. These changes are an attempt to optimize photosynthesis and increase energy sinks for excess reductant, while minimizing photooxidative stress. A transfer to very-low light resulted in a lower photosynthetic performance and metabolic alteration, reflecting an energy-limited state. Genes located on the nucleomorph, the vestigial nucleus in the plastid, had few changes in expression in either light treatment, indicating this organelle has relinquished most transcriptional control to the nucleus. Overall, during plastid origin, both host and transferred endosymbiont genes evolved a harmonized transcriptional network to respond to a classic photosynthetic stress.

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“…A number of other sHsps have been reported to be localized in mitochondria; these include a 22-kDa temperature-induced protein in Leishmania (45), an Hsp22 in pea leaves (46), an Hsp22 with a putative mitochondrial transit signal in soybean (47), a light-stress regulated Hsp of 23 kDa in Chenopodium rubrum (48), and an Hsp30 in Neurospora crassa (49). A cytosolic Hsp22 induced by oxidative stress in Lycopersicon esculentum and presumed to be mitochondrial on the basis of its partial homology with C. rubrum Hsp23 (50) may be identical with Hsp23.8, the gene for which shows a mitochondrial target signal using PSORT software analysis (51).…”

Section: Dmhsp22: a Small Heat Shock Protein In D Melanogastermentioning

confidence: 99%

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

Morrow

Inaguma

Kato

et al. 2000

Journal of Biological Chemistry

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Drosophila melanogaster has four main small heat shock proteins (Hsps), D. melanogaster Hsp22 (DmHsp22), Hsp23 (DmHsp23), Hsp26 (DmHsp26), and Hsp27 (DmHsp27). These proteins, although they have high sequence homology, show distinct developmental expression patterns. The function(s) of each small heat shock protein is unknown. DmHsp22 is shown to localize in mitochondria both in D. melanogaster S2 cells and after heterologous expression in mammalian cells. Fractionation of mitochondria indicates that DmHsp22 resides in the mitochondrial matrix, where it is found in oligomeric complexes, as shown by sedimentation and gel filtration analysis and by cross-linking experiments. Deletion analysis using a DmHsp22-EGFP construct reveals that residues 1-17 and an unknown number of residues between 17-28 are necessary for import. Sitedirected mutagenesis within a putative mitochondrial motif (WRMAEE) at positions 8 -13 shows that the first four residues are necessary for mitochondrial localization. Immunoprecipitation results indicate that there is no interaction between DmHsp22 and the other small heat shock proteins. The mitochondrial localization of this small Hsp22 of Drosophila and its high level of expression in aging suggests a role for this small heat shock protein in protection against oxidative stress.Exposure of organisms to various stresses activates a subset of genes encoding for phylogenically conserved proteins known as the heat shock proteins (Hsps).1 These proteins are commonly divided into families on the basis of molecular weight and sequence homologies. Members of the Hsp70, Hsp90, and Hsp60 families have been shown to act as molecular chaperones in protein folding or refolding following aggregation, and some assist protein translocation through a number of cellular membrane systems. Their chaperone activities are ATP-dependent, and the process is often assisted by co-chaperones. The sHsps comprise a more diverse and less conserved group of proteins, the number and sequences of which vary between and within species. They share a common structural domain in their C termini that shows high homology to the ␣A-and ␣B-crystallins (1). There is evidence for a chaperone-like activity of some sHsps in vitro, where they have been shown to interact with nonnative proteins in an ATP-independent manner (2-5). However, sHsps seem to be rather inefficient chaperones, and they have been suggested to act as reservoirs of nonnative refoldable proteins, which can be refolded in collaboration with other chaperones, such as Hsp70 (6, 7).The role(s) of sHsps in vivo remain unclear. Landry et al. (8) reported that overexpression of human Hsp27 could protect cells from the adverse effects of heat, a phenomenon referred to as thermotolerance. One of the sHsps of Drosophila melanogaster, DmHsp27, also conferred thermal resistance in the same assay (9). This finding is consistent with an early report (10) showing that induction of the Drosophila sHsps by the molting hormone ecdysone was sufficient to confer a thermostable phe...

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

Cited by 14 publications

References 32 publications

Identification of stress‐induced mitochondrial proteins in cultured tobacco cells

Identification of stress‐induced mitochondrial proteins in cultured tobacco cells

Transcriptome Profiling of Bigelowiella natans in Response to Light Stress

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

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