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Molecular chaperones: assisting assembly in addition to folding
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Ellis, R. John (2006) Molecular chaperones: assisting assembly in addition to folding. TRENDS IN BIOCHEMICAL SCIENCES, 31 (7). pp. 395-401. doi:10.1016/j.tibs.2006.05.001
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Official URL: http://dx.doi.org/10.1016/j.tibs.2006.05.001
Abstract
The common perception that molecular chaperones are involved primarily with assisting the folding of newly synthesized and stress-denatured polypeptide chains ignores the fact that this term was invented to describe the function of a protein that assists the assembly of folded subunits into oligomeric structures and only later was extended to embrace protein folding. Recent work has clarified the role of nuclear chaperones in the assembly of nucleosomes and has identified a cytosolic chaperone required for mammalian proteasome assembly, suggesting that the formation of other oligomeric complexes might be assisted by chaperones.
Item Type: | Journal Item | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | TRENDS IN BIOCHEMICAL SCIENCES | ||||
Publisher: | ELSEVIER SCIENCE LONDON | ||||
ISSN: | 0968-0004 | ||||
Official Date: | July 2006 | ||||
Dates: |
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Volume: | 31 | ||||
Number: | 7 | ||||
Number of Pages: | 7 | ||||
Page Range: | pp. 395-401 | ||||
DOI: | 10.1016/j.tibs.2006.05.001 | ||||
Publication Status: | Published |
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