Source:http://linkedlifedata.com/resource/pubmed/id/10962105
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2000-10-16
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| pubmed:abstractText |
The small heat-shock protein (sHsp), alpha-crystallin, acts as a molecular chaperone by interacting with destabilized 'substrate' proteins to prevent their precipitation from solution under conditions of stress. alpha-Crystallin and all sHsps are intracellular proteins. Similarly to other chaperones, the 'substrate' protein is in an intermediately folded, partly structured molten globule state when it interacts and complexes with alpha-crystallin. In this study, stable molten globule states of the cytosolic proteins, gamma-crystallin and myoglobin, have been prepared. Within the lens, gamma-crystallin naturally interacts with alpha-crystallin and myoglobin and alpha-crystallin are present together in muscle tissue. The molten globule states of gamma-crystallin and myoglobin were prepared by reacting gamma-crystallin with glucose 6-phosphate and by removing the haem group of myoglobin. Following spectroscopic characterisation of these modified proteins, their interaction with alpha-crystallin was examined by a variety of spectroscopic and protein chemical techniques. In both cases, there was no interaction with alpha-crystallin that led to complexation. It is concluded that alpha-crystallin does not recognise stable molten globule states of cytosolic 'substrate' proteins and only interacts with molten globule states of proteins that are on the irreversible pathway towards an aggregated and precipitated form.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-anilino-8-naphthalenesulfonate,
http://linkedlifedata.com/resource/pubmed/chemical/Anilino Naphthalenesulfonates,
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose-6-Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Myoglobin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0006-3002
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
31
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| pubmed:volume |
1481
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
175-88
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10962105-Anilino Naphthalenesulfonates,
pubmed-meshheading:10962105-Animals,
pubmed-meshheading:10962105-Binding Sites,
pubmed-meshheading:10962105-Cattle,
pubmed-meshheading:10962105-Circular Dichroism,
pubmed-meshheading:10962105-Crystallins,
pubmed-meshheading:10962105-Cytosol,
pubmed-meshheading:10962105-Fluorescent Dyes,
pubmed-meshheading:10962105-Glucose-6-Phosphate,
pubmed-meshheading:10962105-Glycoproteins,
pubmed-meshheading:10962105-Glycosylation,
pubmed-meshheading:10962105-Heat-Shock Proteins,
pubmed-meshheading:10962105-Lens, Crystalline,
pubmed-meshheading:10962105-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10962105-Molecular Chaperones,
pubmed-meshheading:10962105-Molecular Weight,
pubmed-meshheading:10962105-Myoglobin,
pubmed-meshheading:10962105-Protein Folding,
pubmed-meshheading:10962105-Spectrometry, Fluorescence,
pubmed-meshheading:10962105-Spectrometry, Mass, Secondary Ion,
pubmed-meshheading:10962105-Temperature
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| pubmed:year |
2000
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| pubmed:articleTitle |
The small heat-shock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins.
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| pubmed:affiliation |
Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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