Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells

Willsie, Julia K.; Clegg, James S.

doi:10.1002/jcb.10040

Cited by 67 publications

(30 citation statements)

References 96 publications

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“…When compared with the nuclear matrix fractions of human peripheral blood cells, the presence of molecular chaperones (Tcp-1-related protein and certain members of the heat shock protein family) and protein folding catalysts was found to be common with our study (38). The association of heat shock proteins with nuclear matrix fractions has also been shown in cancer and stressed cells (37,41). The presence of topoisomerases in the nuclear matrix fractions shown by earlier studies is yet another feature consistent with our study (42).…”

Section: Discussionsupporting

confidence: 66%

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Nuclear Matrix Proteome Analysis of Drosophila melanogaster

Kallappagoudar

Varma

Pathak

et al. 2010

Molecular & Cellular Proteomics

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The nucleus is a highly structured organelle and contains many functional compartments. Although the structural basis for this complex spatial organization of compartments is unknown, a major component of this organization is likely to be the non-chromatin scaffolding called nuclear matrix (NuMat). Experimental evidence over the past decades indicates that most of the nuclear functions are at least transiently associated with the NuMat, although the components of NuMat itself are poorly known. Here, we report NuMat proteome analysis from Drosophila melanogaster embryos and discuss its links with nuclear architecture and functions. In the NuMat proteome, we found structural proteins, chaperones, DNA/RNAbinding proteins, chromatin remodeling and transcription factors. This complexity of NuMat proteome is an indicator of its structural and functional significance. The eukaryotic cell nucleus contains a number of structural features like heterochromatin, nucleolus, nuclear lamina, and nuclear territories and functional features like transcription foci, replication foci, Cajal bodies, stress-induced foci, etc.(1-7). Packaging of the genome on the other hand also results in non-random distribution of a variety of structural features like chromatin domains that help to regulate expression of genes (8). How these complex structural and functional domains are established and maintained is not known. It is likely that the non-chromatin scaffolding called nuclear matrix (9) plays an important role in this process. Nuclear matrix (NuMat) 1 mainly consists of the nuclear lamina, the nucleolar remnants, and an internal nuclear meshwork of fibers of unknown constitution that can be seen by electron microscopy (10). These fibers have ultrastructural features reminiscent of intermediate filaments of the cytosol (11). The protein component of nucleoplasmic filaments, however, is largely unknown. Earlier studies on a few proteins isolated from nuclear matrix from different organisms have shown them to be DNA-and RNA-binding and structural components of the nuclear pore complex (12), enzymes (13), and nuclear membrane proteins (14). This diversity among the small number of identified NuMat constituents reflects the link of nuclear architecture with the variety of nuclear functions. The importance of NuMat constituents in nuclear processes has been apparent for a long time, and several studies have been carried out to identify the proteins of this complex structure in different organisms (15-18). Major advancements in the field of proteomics now provide further scope for extensive analysis of NuMat in this context.Here, we present a comprehensive analysis of the NuMat proteome of Drosophila melanogaster. NuMat preparations from D. melanogaster embryos were separated by one-dimensional gel electrophoresis, and the proteins were identified by LC-MS/MS. We also report a remarkable variation in the NuMat proteome depending on developmental stages, indicating a link between embryonic development and nuclear architecture. Finally, immunos...

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Section: Discussionsupporting

confidence: 66%

“…It has been shown in many earlier studies that heat shock proteins and other chaperones are associated with nuclear matrix (37,38). It has also been shown in a recent study that molecular chaperone Hsp90 interacts with Trithorax to maintain active chromatin at sites of gene expression (39).…”

Section: Discussionmentioning

confidence: 97%

Nuclear Matrix Proteome Analysis of Drosophila melanogaster

Kallappagoudar

Varma

Pathak

et al. 2010

Molecular & Cellular Proteomics

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“…A massive accumulation of the sHsp p26 occurs in diapausing embryos of this brine shrimp (Liang et al 1997a;Liang et al 1997b). The protein p26 is able to move into the nucleus (Clegg et al 1995) and is thought to protect and/or chaperone, in cooperation with Hsp70, the nuclear matrix proteins (Willsie and Clegg 2002).…”

Section: Discussionmentioning

confidence: 99%

Stress response in tardigrades: differential gene expression of molecular chaperones

Reuner

Hengherr

Mali

et al. 2010

Cell Stress and Chaperones

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Semi-terrestrial tardigrades exhibit a remarkable tolerance to desiccation by entering a state called anhydrobiosis. In this state, they show a strong resistance against several kinds of physical extremes. Because of the probable importance of stress proteins during the phases of dehydration and rehydration, the relative abundance of transcripts coding for two α-crystallin heat-shock proteins (MtsHsp17.2 and Mt-sHsp19.5), as well for the heat-shock proteins Mt-sHsp10, Mt-Hsp60, Mt-Hsp70 and Mt-Hsp90, were analysed in active and anhydrobiotic tardigrades of the species Milnesium tardigradum. They were also analysed in the transitional stage (I) of dehydration, the transitional stage (II) of rehydration and in heat-shocked specimens. A variable pattern of expression was detected, with most candidates being downregulated. Gene transcripts of one Mt-hsp70 isoform in the transitional stage I and Mt-hsp90 in the anhydrobiotic stage were significantly upregulated. A high gene expression (778.6-fold) was found for the small α-crystallin heat-shock protein gene Mt-sHsp17.2 after heat shock. We discuss the limited role of the stress-gene expression in the transitional stages between the active and anhydrobiotic tardigrades and other mechanisms which allow tardigrades to survive desiccation.

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“…Remarkably, these ''encysted'' embryos can survive years of continuous anoxia (60), desiccation, and UV radiation (57). Major adaptations include massive accumulation of the sugar trehalose, which helps offset desiccation, and the synthesis and accumulation in the nucleus of an HSP (p26), which is thought to protect the nuclear proteins during these extreme conditions (61). A different developmental approach is seen in C. elegans.…”

Section: Alternative Developmental Pathwaysmentioning

confidence: 99%

Embryo stability and vulnerability in an always changing world

Hamdoun

Epel

2007

Proc. Natl. Acad. Sci. U.S.A.

320

266

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Contrary to the view that embryos and larvae are the most fragile stages of life, development is stable under real-world conditions. Early cleavage embryos are prepared for environmental vagaries by having high levels of cellular defenses already present in the egg before fertilization. Later in development, adaptive responses to the environment either buffer stress or produce alternative developmental phenotypes. These buffers, defenses, and alternative pathways set physiological limits for development under expected conditions; teratology occurs when embryos encounter unexpected environmental changes and when stress exceeds these limits. Of concern is that rapid anthropogenic changes to the environment are beyond the range of these protective mechanisms.

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Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells

Cited by 67 publications

References 96 publications

Nuclear Matrix Proteome Analysis of Drosophila melanogaster

Nuclear Matrix Proteome Analysis of Drosophila melanogaster

Stress response in tardigrades: differential gene expression of molecular chaperones

Embryo stability and vulnerability in an always changing world

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