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.abs

Cited by 14 publications

(17 citation statements)

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“…Two putative chaperone proteins were identified in this study, the Arabidopsis HSP/HSC70 homolog At‐hsc70‐3, and the Arabidopsis homolog of DNAj (atj3), a co‐chaperone of the yeast HSP/HSC70 homolog DnaK. Brine shrimp ( Artemia franciscana ) HSP70 has been shown to associate with the small heat shock protein p26 and with nuclear lamins within the context of the nuclear matrix, presumably preventing protein unfolding upon cellular stress [Willsie and Clegg, 2002]. Similar results were also obtained in other experimental animal and human systems [Pouchelet et al, 1983; Gerner et al, 1999; Gerner et al, 2002].…”

Section: Discussionmentioning

confidence: 99%

A proteomic study of the arabidopsis nuclear matrix

Calikowski

Meulia

Meier³

2003

J of Cellular Biochemistry

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The eukaryotic nucleus has been proposed to be organized by two interdependent nucleoprotein structures, the DNA-based chromatin and the RNA-dependent nuclear matrix. The functional composition and molecular organization of the second component have not yet been resolved. Here, we describe the isolation of the nuclear matrix from the model plant Arabidopsis, its initial characterization by confocal and electron microscopy, and the identification of 36 proteins by mass spectrometry. Electron microscopy of resinless samples confirmed a structure very similar to that described for the animal nuclear matrix. Two-dimensional gel electrophoresis resolved approximately 300 protein spots. Proteins were identified in batches by ESI tandem mass spectrometry after resolution by 1D SDS-PAGE. Among the identified proteins were a number of demonstrated or predicted Arabidopsis homologs of nucleolar proteins such as IMP4, Nop56, Nop58, fibrillarins, nucleolin, as well as ribosomal components and a putative histone deacetylase. Others included homologs of eEF-1, HSP/HSC70, and DnaJ, which have also been identified in the nucleolus or nuclear matrix of human cells, as well as a number of novel proteins with unknown function. This study is the first proteomic approach towards the characterization of a higher plant nuclear matrix. It demonstrates the striking similarities both in structure and protein composition of the operationally defined nuclear matrix across kingdoms whose unicellular ancestors have separated more than one billion years ago.

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Section: Discussionmentioning

confidence: 99%

A proteomic study of the arabidopsis nuclear matrix

Calikowski

Meulia

Meier³

2003

J of Cellular Biochemistry

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“…On the other hand, the p26 could be transferred directly into the nuclei by the endosomes that transport it across the plasma membrane. We have shown that p26 binds tightly to nuclear lamins in Artemia embryo cell nuclei (Willsie and Clegg, 2002). If that is the case in the transduced Cos-1 cells, such binding would account for p26 retention in nuclei ( Figs.…”

Section: Discussionmentioning

confidence: 71%

“…Artemia embryos are among the most stress-resistant of all animal life history stages (reviewed by Clegg and Trotman, 2002), in part because they contain massive amounts of a small stress protein, p26, and very high concentrations of trehalose. Much information has been obtained about Artemia p26 since its initial description (Clegg et al, 1994(Clegg et al, , 1995, and more recently (Crack et al, 2002;Willsie and Clegg, 2002).…”

Section: Introductionmentioning

confidence: 99%

A small heat‐shock protein, p26, from the crustacean Artemia protects mammalian cells (Cos‐1) against oxidative damage

Collins

Clegg

2004

Cell Biology International

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A small heat-shock protein (p26) purified from stress-resistant embryos of the crustacean, Artemia franciscana, was introduced into cultured cells of green monkey kidney (Cos-1) using the BioPORTER delivery system. Cells containing p26 exhibited impressive resistance to hydrogen peroxide compared to controls. Introduction of the disaccharide trehalose did not provide protection against oxidative damage, but enhanced substantially the protective performance of p26 when both were present. These studies extend previous research on the protective role played by p26 in cells exposed to various forms of stress, presumably through its ability to function as a molecular chaperone.

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“…Artemin and p26, the latter a small heat shock/a-crystallin protein from Artemia with molecular chaperone activity, reside in developing Artemia at similar times [8,10,12,13,51]. Artemin may also be a molecular chaperone whose activity, like Hsp33, is redox controlled [52,53].…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of artemin and ferritin from Artemia franciscana

Chen

Amons

Clegg

et al. 2002

European Journal of Biochemistry

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Embryos of the brine shrimp, Artemia franciscana, exhibit remarkable resistance to physiological stress, which is temporally correlated with the presence of two proteins, one a small heat shock/a-crystallin protein termed p26 and the other called artemin, of unknown function. Artemin was sequenced previously by Edman degradation, and its relationship to ferritin, an iron storage protein, established. The isolation from an Artemia expressed sequence tag library of artemin and ferritin cDNAs extends this work. Artemin cDNA was found to contain an ORF of 693 nucleotides, and its deduced amino-acid sequence, except for the initiator methionine, was identical with that determined previously. Ferritin cDNA is 725 bp in length with an ORF of 516 nucleotides. Artemin amino-acid residues 32-185 are most similar to ferritin, but artemin is enriched in cysteines. The abundance of cysteines and their intramolecular spatial distribution suggest that artemin protects embryos against oxidative damage and/or that its function is redox regulated.The conserved regions in artemin and ferritin monomers are structurally similar to one another and both proteins assemble into oligomers. However, modeling of the quaternary structure indicated that artemin multimers lack the central space used for metal storage that characterizes ferritin oligomers, implying different roles for this protein.Probing of Northern blots revealed two artemin transcripts, one of 3.5 kb and another of 2.2 kb. These transcripts decreased in parallel and had almost disappeared by 16 h of development. The ferritin transcript of 0.8 kb increased slightly during reinitiation of development, then declined, and was almost completely gone by 16 h. Clearly, the loss of artemin and ferritin during embryo development is due to transcriptional regulation and proteolytic degradation of the proteins.

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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 14 publications

References 0 publications

A proteomic study of the arabidopsis nuclear matrix

A proteomic study of the arabidopsis nuclear matrix

A small heat‐shock protein, p26, from the crustacean Artemia protects mammalian cells (Cos‐1) against oxidative damage

Molecular characterization of artemin and ferritin from Artemia franciscana

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