Journal
FEBS LETTERS
Volume 583, Issue 1, Pages 88-92Publisher
WILEY
DOI: 10.1016/j.febslet.2008.11.049
Keywords
Janus chaperone; Ribosomal protein; Intrinsically disordered proteins
Funding
- Hungarian Scientific Research Fund [OTKA K60694, NK71582]
- Hungarian Ministry of Health [ETT 245/2006]
- International Senior Research Fellowship ISRF [067595]
- Wellcome Trust
- Austrian Science Fund (FWF) [W1207] Funding Source: Austrian Science Fund (FWF)
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Ribosomal proteins assist the assembly and increase the stability of ribosomal RNA, without requiring ATP for their action. Some ribosomal proteins are also known to have essential functions outside the ribosome, i.e. promiscuity of functions that appears to correlate with their structural disorder. Here we addressed if certain ribosomal proteins with RNA chaperone activity and with a significant level of disorder also have protein-chaperone activity in vitro. Four proteins of the large subunit of Escherichia coli ribosome, L15, L16, L18 and L19 have been tested in three chaperone assays, in which all of them exhibited potent chaperone activity, commensurable with that of heat shock protein 90 kDa. These observations highlight possible novel aspects of the promiscuous functions of ribosomal proteins outside of the ribosome. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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