Free Human Mitochondrial Grpe Is A Symmetric Dimer In Solution.

dc.creatorBorges, Júlio C
dc.creatorFischer, Hannes
dc.creatorCraievich, Aldo F
dc.creatorHansen, Lee D
dc.creatorRamos, Carlos H I
dc.date2003-Sep
dc.date2015-11-27T12:52:14Z
dc.date2015-11-27T12:52:14Z
dc.date.accessioned2018-03-29T00:57:37Z
dc.date.available2018-03-29T00:57:37Z
dc.identifierThe Journal Of Biological Chemistry. v. 278, n. 37, p. 35337-44, 2003-Sep.
dc.identifier0021-9258
dc.identifier10.1074/jbc.M305083200
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/12840016
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195430
dc.identifier12840016
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295663
dc.descriptionThe co-chaperone GrpE is essential for the activities of the Hsp70 system, which assists protein folding. GrpE is present in several organisms, and characterization of homologous GrpEs is important for developing structure-function relationships. Cloning, producing, and conformational studies of the recombinant human mitochondrial GrpE are reported here. Circular dichroism measurements demonstrate that the purified protein is folded. Thermal unfolding of human GrpE measured both by circular dichroism and differential scanning calorimetry differs from that of prokaryotic GrpE. Analytical ultracentrifugation data indicate that human GrpE is a dimer, and the sedimentation coefficient agrees with an elongated shape model. Small angle x-ray scattering analysis shows that the protein possesses an elongated shape in solution and demonstrates that its envelope, determined by an ab initio method, is similar to the high resolution envelope of Escherichia coli GrpE bound to DnaK obtained from single crystal x-ray diffraction. However, in these conditions, the E. coli GrpE dimer is asymmetric because the monomer that binds DnaK adopts an open conformation. It is of considerable importance for structural GrpE research to answer the question of whether the GrpE dimer is only asymmetric while bound to DnaK or also as a free dimer in solution. The low resolution structure of human GrpE presented here suggests that GrpE is a symmetric dimer when not bound to DnaK. This information is important for understanding the conformational changes GrpE undergoes on binding to DnaK.
dc.description278
dc.description35337-44
dc.languageeng
dc.relationThe Journal Of Biological Chemistry
dc.relationJ. Biol. Chem.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectCalorimetry, Differential Scanning
dc.subjectCircular Dichroism
dc.subjectCloning, Molecular
dc.subjectComputer Simulation
dc.subjectDna Primers
dc.subjectDimerization
dc.subjectHeat-shock Proteins
dc.subjectHumans
dc.subjectMitochondria
dc.subjectMolecular Chaperones
dc.subjectMolecular Sequence Data
dc.subjectPolymerase Chain Reaction
dc.subjectProtein Conformation
dc.subjectProtein Folding
dc.subjectRecombinant Proteins
dc.subjectSequence Alignment
dc.subjectSequence Homology, Amino Acid
dc.subjectSolutions
dc.subjectThermodynamics
dc.subjectX-ray Diffraction
dc.titleFree Human Mitochondrial Grpe Is A Symmetric Dimer In Solution.
dc.typeArtículos de revistas


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