ArticleRNA (New York, N.Y.)2009
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- Inter-domain communication in the dimeric DEAD-box helicase Hera from T. thermophilus and implications for the mechanism of RNA unwinding.Nucleic acids research · 2025Article
- TheRNA (New York, N.Y.) · 2020Article
- Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera.Nucleic acids research · 2013Article
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- Structural and functional analysis of the archaeal endonuclease Nob1.Nucleic acids research · 2012Article
- From unwinding to clamping - the DEAD box RNA helicase family.Nature reviews. Molecular cell biology · 2011Review
- Phylogenetic distribution and evolutionary history of bacterial DEAD-Box proteins.Journal of molecular evolution · 2011Article
- Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases.Biochemical Society transactions · 2011Review
- DEAD-box proteins as RNA helicases and chaperones.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEAD box family helicases consist of a helicase core that is formed by two flexibly linked RecA-like domains. The helicase activity can be regulated by N- or C-terminal extensions flanking the core. Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) is the first DEAD box helicase that forms a dimer using a unique dimerization domain. In addition to the dimerization domain, Hera contains a C-terminal RNA binding domain (RBD) that shares sequence homology only to uncharacterized proteins of the Deinococcus/Thermus group. The crystal structure of Hera_RBD reveals the fold of an altered RNA recognition motif (RRM) with limited structural homology to the RBD of the DEAD box helicase YxiN from Bacillus subtilis. Comparison with RRM/RNA complexes shows that a RNA binding mode different than that suggested for YxiN, but similar to U1A, can be inferred for Hera. The orientation of the RBD relative to the helicase core was defined in a second crystal structure of a Hera fragment including the C-terminal RecA domain, the dimerization domain, and the RBD. The structures allow construction of a model for the entire Hera helicase dimer. A likely binding surface for large RNA substrates that spans both RecA-like domains and the RBD is identified.
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