Back to Search
Start Over
A guanosine-centric mechanism for RNA chaperone function.
- Source :
-
Science (New York, N.Y.) [Science] 2013 Apr 12; Vol. 340 (6129), pp. 190-5. Date of Electronic Publication: 2013 Mar 07. - Publication Year :
- 2013
-
Abstract
- RNA chaperones are ubiquitous, heterogeneous proteins essential for RNA structural biogenesis and function. We investigated the mechanism of chaperone-mediated RNA folding by following the time-resolved dimerization of the packaging domain of a retroviral RNA at nucleotide resolution. In the absence of the nucleocapsid (NC) chaperone, dimerization proceeded through multiple, slow-folding intermediates. In the presence of NC, dimerization occurred rapidly through a single structural intermediate. The RNA binding domain of heterogeneous nuclear ribonucleoprotein A1 protein, a structurally unrelated chaperone, also accelerated dimerization. Both chaperones interacted primarily with guanosine residues. Replacing guanosine with more weakly pairing inosine yielded an RNA that folded rapidly without a facilitating chaperone. These results show that RNA chaperones can simplify RNA folding landscapes by weakening intramolecular interactions involving guanosine and explain many RNA chaperone activities.
- Subjects :
- Base Sequence
Dimerization
Guanosine chemistry
Heterogeneous Nuclear Ribonucleoprotein A1
Heterogeneous-Nuclear Ribonucleoprotein Group A-B chemistry
Heterogeneous-Nuclear Ribonucleoprotein Group A-B metabolism
Inosine chemistry
Inosine metabolism
Kinetics
Models, Molecular
Molecular Chaperones chemistry
Moloney murine leukemia virus genetics
Nucleic Acid Conformation
Nucleocapsid Proteins chemistry
Protein Binding
RNA, Viral metabolism
Guanosine metabolism
Molecular Chaperones metabolism
Moloney murine leukemia virus metabolism
Nucleocapsid Proteins metabolism
RNA, Viral chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 340
- Issue :
- 6129
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 23470731
- Full Text :
- https://doi.org/10.1126/science.1230715