Article ; Online: Dead or alive: DEAD-box ATPases as regulators of ribonucleoprotein complex condensation.
2021 Volume 402, Issue 5, Page(s) 653–661
Abstract: DEAD-box ATPase proteins are found in all clades of life and have been associated with a diverse array of RNA-processing reactions in eukaryotes, bacteria and archaea. Their highly conserved core enables them to bind RNA, often in an ATP-dependent manner. ...
Abstract | DEAD-box ATPase proteins are found in all clades of life and have been associated with a diverse array of RNA-processing reactions in eukaryotes, bacteria and archaea. Their highly conserved core enables them to bind RNA, often in an ATP-dependent manner. In the course of the ATP hydrolysis cycle, they undergo conformational rearrangements, which enable them to unwind short RNA duplexes or remodel RNA-protein complexes. Thus, they can function as RNA helicases or chaperones. However, when their conformation is locked, they can also clamp RNA and create ATP-dependent platforms for the formation of higher-order ribonucleoprotein complexes. Recently, it was shown that DEAD-box ATPases globally regulate the phase-separation behavior of RNA-protein complexes |
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MeSH term(s) | Adenosine Triphosphatases/metabolism ; DEAD-box RNA Helicases/metabolism ; Hydrolysis ; Models, Molecular ; Protein Conformation ; Ribonucleoproteins/metabolism |
Chemical Substances | Ribonucleoproteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13) |
Language | English |
Publishing date | 2021-04-02 |
Publishing country | Germany |
Document type | Journal Article ; Research Support, Non-U.S. Gov't ; Review |
ZDB-ID | 1334659-3 |
ISSN | 1437-4315 ; 1431-6730 ; 1432-0355 |
ISSN (online) | 1437-4315 |
ISSN | 1431-6730 ; 1432-0355 |
DOI | 10.1515/hsz-2020-0381 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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