関: GroES protein

WordNet

one who accompanies and supervises a young woman or gatherings of young people (同)chaperone

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/04/22 09:16:03」(JST)

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Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL.^[1]

GroES exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits.^[2] These ring structures assemble by self-stimulation in the presence of Mg²⁺-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg²⁺-ATP dependent manner.^[3] The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.

Escherichia coli GroES has also been shown to bind ATP cooperatively, and with an affinity comparable to that of GroEL.^[4] Each GroEL subunit contains three structurally distinct domains: an apical, an intermediate and an equatorial domain. The apical domain contains the binding sites for both GroES and the unfolded protein substrate. The equatorial domain contains the ATP-binding site and most of the oligomeric contacts. The intermediate domain links the apical and equatorial domains and transfers allosteric information between them. The GroEL oligomer is a tetradecamer, cylindrically shaped, that is organised in two heptameric rings stacked back to back. Each GroEL ring contains a central cavity, known as the `Anfinsen cage', that provides an isolated environment for protein folding. The identical 10 kDa subunits of GroES form a dome-like heptameric oligomer in solution. ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP, to facilitate cooperative ATP binding and hydrolysis for substrate protein release.

Interactions

GroES has been shown to interact with GroEL.^[5]^[6]

References

^ "Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)".
^ Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature 333 (6171): 330–4. doi:10.1038/333330a0. PMID 2897629.
^ Schmidt A, Schiesswohl M, Volker U, Hecker M, Schumann W (June 1992). "Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis". J. Bacteriol. 174 (12): 3993–9. PMC 206108. PMID 1350777.
^ Martin J, Geromanos S, Tempst P, Hartl FU (November 1993). "Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES". Nature 366 (6452): 279–82. doi:10.1038/366279a0. PMID 7901771.
^ Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (April 1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
^ Lee KH, Kim HS, Jeong HS, Lee YS (October 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. doi:10.1016/S0006-291X(02)02423-3. PMID 12387818.

External links

GroES Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
3D macromolecular structures of GroES in EMDB

This article on a gene on chromosome 2 is a stub. You can help Wikipedia by expanding it.

This article incorporates text from the public domain Pfam and InterPro IPR020818

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English Journal

Screening on human hepatoma cell line HepG-2 nucleus and cytoplasm protein after CDK2 silencing by RNAi.

Han X1, Wang Z, Wang W, Bai R, Zhao P, Shang J.
Cytotechnology.Cytotechnology.2014 Aug;66(4):567-74. doi: 10.1007/s10616-013-9604-0. Epub 2014 May 7.
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PMID 24801578

Chaperonins resculpt folding free energy landscapes to avoid kinetic traps and accelerate protein folding.

Zhang X1, Kelly JW2.
Journal of molecular biology.J Mol Biol.2014 Jul 29;426(15):2736-8. doi: 10.1016/j.jmb.2014.06.001. Epub 2014 Jun 5.
PMID 24909364

Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.

Gupta AJ1, Haldar S1, Miličić G1, Hartl FU2, Hayer-Hartl M3.
Journal of molecular biology.J Mol Biol.2014 Jul 29;426(15):2739-54. doi: 10.1016/j.jmb.2014.04.018. Epub 2014 May 6.
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coli have an essential role in assisting protein folding by transiently encapsulating non-native substrate in an ATP-regulated mechanism. It remains controversial whether the chaperonin system functions solely as an in
PMID 24816391

Japanese Journal

2Ea10 循環置換型連結変異体によるII型シャペロニンヘテロリング複合体の構築(タンパク質工学,一般講演)

山本陽平,阿部由寛,阿部哲也,養王田正文
日本生物工学会大会講演要旨集 63, 143, 2011-08-25
NAID 110008911376

Differential protein profiles of Bradyrhizobium japonicum USDA110 bacteroid during soybean nodule development(Soil Biology)

Nomura Mika,Arunothayanan Hatthaya,Dao Tan Van [他],LE Hoa Thi-Phuong,KANEKO Takakazu,SATO Shusei,TABATA Satoshi,TAJIMA Shigeyuki
Soil science and plant nutrition 56(4), 579-590, 2010-08-00
… Using proteomic analysis, protein expressions in soybean nodule bacteroids 7, 10, 14, 28, and 49 days after inoculation (DAI) were monitored. … The time points coincide with the early stage of nodule formation (7-10 DAI), the onset of nitrogen fixation (14-28 DAI), and nodule senescence (49 DAI). …
NAID 110008144356

Synthesis of 4-Pyridoxolactone from Pyridoxine Using a Combination of Transformed Escherichia coli Cells(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Tamura Asuka,Yoshikane Yu,Yokochi Nana [他],Yagi Toshiharu
Journal of bioscience and bioengineering 106(5), 460-465, 2008-11-25
… One set of transformed cells expressed pyridoxine 4-oxidase, catalase, and chaperonin, while the second set expressed pyridoxal 4-dehydrogenase. … In a reaction mixture containing the two transformed cell types, 10mM of pyridoxine was completely converted into 4-pyridoxolactone at 30℃ in 24h. …
NAID 110007005171

Related Pictures

★リンクテーブル★

リンク元	「シャペロニン10」「GroES protein」

「シャペロニン10」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Cpn10
	; gp31 co-chaperonin from bacteriophage t4
Identifiers
Symbol	Cpn10
Pfam	PF00166
Pfam clan	CL0296
InterPro	IPR020818
PROSITE	PDOC00576
SCOP	1lep
SUPERFAMILY	1lep
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Heat shock 10kDa protein 1 (chaperonin 10)
Identifiers
Symbols	HSPE1; CPN10; EPF; GROES; HSP10
External IDs	OMIM: 600141 MGI: 104680 HomoloGene: 20500 GeneCards: HSPE1 Gene
Gene Ontology
Molecular function	• protein binding; • ATP binding; • unfolded protein binding; • chaperone binding;
Cellular component	• mitochondrion; • mitochondrial matrix;
Biological process	• protein folding; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • response to unfolded protein;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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