Source:http://linkedlifedata.com/resource/pubmed/id/10441154
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
32
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pubmed:dateCreated |
1999-9-8
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pubmed:abstractText |
The backbone dynamics of the N-terminal domain of the chaperone protein Escherichia coli DnaJ have been investigated using steady-state 1H-15N NOEs, 15N T1, T2, and T1 rho relaxation times, steady-state 13C alpha-13CO NOEs, and 13CO T1 relaxation times. Two recombinant constructs of the N-terminal domain of DnaJ have been studied. One, DnaJ(1-78), contains the most conserved "J-domain" of DnaJ, and the other, DnaJ(1-104), includes a glycine/phenylalanine rich region ("G/F" region) in addition to the "J-domain". DnaJ(1-78) is not capable of stimulating ATP hydrolysis by DnaK, despite the fact that all currently identified sites responsible for DnaJ-DnaK interaction are located in this region. DnaJ(1-104), on the other hand, retains nearly the full ATPase stimulatory activity of full length DnaJ. Recently, a structural analysis of these two molecules was presented in an effort to elucidate the origin of their functional differences [Huang, K., Flanagan, J. M., and Prestegard, J. H. (1999) Protein Science 8, 203-214]. Herein, an analysis of dynamic properties is presented in a similar effort. A generalized model-free approach with a full treatment of the anisotropic overall rotation of the proteins is used in the analysis of measured relaxation parameters. Our results show that internal motions on pico- to nanosecond time scales in the backbone of DnaJ(1-78) are reduced on the inclusion of the "G/F" region, while conformational exchange on micro- to millisecond time scales increases. We speculate that the enhanced flexibility of residues on the slow time scale upon the inclusion of the "G/F" region could be relevant to the ATPase stimulatory activity of DnaJ if an "induced-fit" mechanism applies to DnaJ-DnaK interactions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/DnaJ protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10567-77
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pubmed:dateRevised |
2010-5-10
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pubmed:meshHeading |
pubmed-meshheading:10441154-Anisotropy,
pubmed-meshheading:10441154-Bacterial Proteins,
pubmed-meshheading:10441154-Carbon Isotopes,
pubmed-meshheading:10441154-Escherichia coli,
pubmed-meshheading:10441154-Escherichia coli Proteins,
pubmed-meshheading:10441154-HSP40 Heat-Shock Proteins,
pubmed-meshheading:10441154-Heat-Shock Proteins,
pubmed-meshheading:10441154-Models, Chemical,
pubmed-meshheading:10441154-Models, Molecular,
pubmed-meshheading:10441154-Nitrogen Isotopes,
pubmed-meshheading:10441154-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10441154-Peptide Fragments,
pubmed-meshheading:10441154-Protein Conformation,
pubmed-meshheading:10441154-Thermodynamics
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pubmed:year |
1999
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pubmed:articleTitle |
Backbone dynamics of the N-terminal domain in E. coli DnaJ determined by 15N- and 13CO-relaxation measurements.
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pubmed:affiliation |
Complex Carbohydrate Research Center, University of Georgia, Athens 30602-4712, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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