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Effect of TAT-signaling fusion system along with co-expression of GroEL/ES chaperones on secretory expression of somatropin

100%

Rabbani M., Ghasemi R., Bagherinejad M. R., Jahanian A.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2020

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tom 101

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nr 2

2

AtDeg2 - a chloroplast protein with dual protease/chaperone activity

86%

Jagodzik P., Adamiec M., Jackowski G.

Acta Societatis Botanicorum Poloniae

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2014

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tom 83

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nr 3

Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.

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Antibodies to heat shock proteins 90alpha and 90beta in psoriasis

72%

Damasiewicz-Bodzek A., Szumska M., Tyrpien-Golder K.

Archivum Immunologiae et Therapiae Experimentalis

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2020

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tom 68

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nr 2

4

Plasma membrane rafts and chaperones in cytokine STAT signalling

72%

Sehgal P. B.

Acta Biochimica Polonica

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2003

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tom 50

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nr 3

We and others have recently obtained data suggesting that cytokine-STAT signaling in many different cell-types is a chaperoned pathway initiated at the level of specialized plasma membrane microdomains called "rafts" (the "raft-STAT signaling hypothesis"). These findings are of broad significance in that all cytokines and growth factors initiate signaling in target cells by interacting with respective cell-surface receptors. The new data suggest that raft microdomains represent the units of function at the cell-surface through which ligand-stimulated STAT signaling is initiated. Moreover, recent evidence shows the involvement of chaperone proteins in regulating the STAT signaling pathway. These chaperones include the human homolog of the tumorous imaginal disc 1 protein (hTidl) which associates with Janus kinase 2 (JAK2) at the level of the plasma membrane, heat shock protein 90 (HSP90) which associates with STAT3 and STAT1 proteins in caveolin-l-containing raft and cytoplasmic complexes, and glucose regulated protein 58 (GRP58/ER-60/ERp57), a thiol dependent protein-disulfide isomerase, found in association with STAT3 “statosome” complexes in the cytosol and in the raft fraction. We suggest a function of the HSP90 chaperone system in preserving IL-6/STAT3 signaling in liver cells in the context of fever. The identification and function of protein partners associated with specific STAT species in rafts and in cytosolic complexes, and in the efficient departure of cytokine-activated STATs from the cytosolic face of rafts towards the cell nucleus are now areas of active investigation.

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Influence of DnaK and DnaJ chaperones on Escherichia coli membrane lipid composition

72%

Sienczyk J., Sklodowska A., Grudniak A., Wolska K. I.

Polish Journal of Microbiology

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2004

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tom 53

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nr 2

The content of fatty acids extracted from the membranes of E. coli MC1061 harboring the wild-type dnaKdnaJ alleles and its AdnaJ and AdnaKdnaJ derivatives was compared. It was demonstrated that dodecanoic acid was missing in NPLs fraction extracted from both mutants grown at 42°C. Phospholipids extracted from mutant strains were deprived of hexadecanoic acid methyl ester and octadecanol, the latter being correlated with the presence of octadecanoic acid. The amount of LPS extracted from AdnaKdanJ mutant was significantly lower when compared with wild-type strain and AdnaJ mutant.

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Structural basis of the interspecies interaction between the chaperone DnaK[Hsp70] and the co-chaperone GrpE of archaea and bacteria

72%

Zmijewski M. A., Skorsko-Glonek J., Tanfani F., Banecki B., Kotlarz A., Macario A. J. L., Lipinska B.

Acta Biochimica Polonica

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2007

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tom 54

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nr 2

Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK) chaperones cooperate with a GrpE co-chaperone which stimulates the ATPase activity of the DnaK protein. It is currently believed that the archaeal Hsp70 system was obtained by the lateral transfer of chaperone genes from bacteria. Our previous finding that the DnaK and GrpE proteins of M. mazei can functionally cooperate with the Escherichia coli GrpE and DnaK supported this hypothesis. However, the cooperation was surprising, considering the very low identity of the GrpE proteins (26%) and the relatively low identity of the DnaK proteins (56%). The aim of this work was to investigate the molecular basis of the observed interspecies chaperone interaction. Infrared resolution-enhanced spectra of the M. mazei and E. coli DnaK proteins were almost identical, indicating high similarity of their secondary structures, however, some small differences in band position and in the intensity of amide I' band components were observed and discussed. Profiles of thermal denaturation of both proteins were similar, although they indicated a higher thermostability of the M. mazei DnaK compared to the E. coli DnaK. Electrophoresis under non-denaturing conditions demonstrated that purified DnaK and GrpE of E. coli and M. mazei formed mixed complexes. Protein modeling revealed high similarity of the 3-dimensional structures of the archaeal and bacterial DnaK and GrpE proteins.

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The chloroplast thiol-disulphide redox regulatory network and the sensory roles of 2-cysteine peroxiredoxin and cyclophilin 20-3

58%

Dietz K.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 2

8

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer

58%

Ruckova E., Muller P., Nenutil R., Vojtesek B.

Cellular and Molecular Biology Letters

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2012

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tom 17

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nr 3

Activation of the Hsp90 chaperone system is a characteristic of cancer cells. The regulation of chaperone activities involves their interaction with cochaperones; therefore we investigated the expression of Hsp70 and Hsp90 and their specific co-chaperones HOP and CHIP in cancer cell lines and primary cancers. Inhibition of Hsp90 by 17AAG increased the levels of Hsp70, Hsp90 and HOP but not CHIP mRNA in cancer cells. These changes are linked to activation of the HSF1 transcription factor and we show that the HOP promoter contains HSF1 binding sites, and that HSF1 binding to the HOP promoter is increased following 17AAG. The lack of alteration in the co-chaperone CHIP is explained by a lack of HSF response elements in the CHIP promoter. Non-proliferating cells expressed higher levels of CHIP and lower HOP, Hsp70 and Hsp90 levels compared to proliferating cells. Decreased expression of CHIP in proliferating cancer cells is in keeping with its proposed tumor suppressor properties, while over-expression of HOP in proliferating cells may contribute to excessive Hsp90 activity and stabilization of client proteins in tumors. In a panel of colorectal cancer samples, increased expression of Hsp70 and an increased ratio of HOP to CHIP were found, and were associated with decreased median survival. These data indicate that multiple changes occur in the chaperone/co-chaperone system in cancer that impact patient survival. It is likely that the ability to identify individual alterations to this system will be beneficial for treatment strategy decisions, particularly those that employ chaperone inhibitors.

Ograniczanie wyników

Effect of TAT-signaling fusion system along with co-expression of GroEL/ES chaperones on secretory expression of somatropin

AtDeg2 - a chloroplast protein with dual protease/chaperone activity

Antibodies to heat shock proteins 90alpha and 90beta in psoriasis

Plasma membrane rafts and chaperones in cytokine STAT signalling

Influence of DnaK and DnaJ chaperones on Escherichia coli membrane lipid composition

Structural basis of the interspecies interaction between the chaperone DnaK[Hsp70] and the co-chaperone GrpE of archaea and bacteria

The chloroplast thiol-disulphide redox regulatory network and the sensory roles of 2-cysteine peroxiredoxin and cyclophilin 20-3

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer