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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2002-1-23
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pubmed:abstractText |
RING domains act in a variety of essential cellular processes but have no general function ascribed to them. Here, we observe that purified arenaviral protein Z, constituted almost entirely by its RING domain, self-assembles in vitro into spherical structures that resemble functional bodies formed by Z in infected cells. By using a variety of biophysical methods we provide a thermodynamic and kinetic framework for the RING-dependent self-assembly of Z. Assembly appears coupled to substantial conformational reorganization and changes in zinc coordination of site II of the RING. Thus, the rate-limiting nature of conformational reorganization observed in the folding of monomeric proteins can also apply to the assembly of macromolecular scaffolds. These studies describe a unique mechanism of nonfibrillar homogeneous self-assembly and suggest a general function of RINGs in the formation of macromolecular scaffolds that are positioned to integrate biochemical processes in cells.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-10233871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-10595557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-10653693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-10708446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11057895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11226167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11320250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11526114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11573085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-11575918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-1230017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-12369920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-1591250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-2435461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-3709531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-3890879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-6615456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-7248451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-7578063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-7729428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-7747483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8240275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8291229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8356089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8561051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8639632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8744354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-8994626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9195890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9241423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9254622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9420283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9525870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9557665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11792829-9653117
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
667-72
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11792829-Amino Acid Sequence,
pubmed-meshheading:11792829-Kinetics,
pubmed-meshheading:11792829-Lassa virus,
pubmed-meshheading:11792829-Lymphocytic choriomeningitis virus,
pubmed-meshheading:11792829-Macromolecular Substances,
pubmed-meshheading:11792829-Microscopy, Electron,
pubmed-meshheading:11792829-Molecular Sequence Data,
pubmed-meshheading:11792829-Protein Conformation,
pubmed-meshheading:11792829-Protein Folding,
pubmed-meshheading:11792829-Protein Structure, Tertiary,
pubmed-meshheading:11792829-Sequence Homology, Amino Acid,
pubmed-meshheading:11792829-Thermodynamics,
pubmed-meshheading:11792829-Viral Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Self-assembly properties of a model RING domain.
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pubmed:affiliation |
Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, New York, NY 10029, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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