Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN.

Nucleic acids research - 1 Jul 2009

Karow Anne R, Klostermeier Dagmar

Abstract excerpt

Cooperative binding of ATP and RNA to DEAD-box helicases induces the closed conformation of their helicase core, with extensive interactions across the domain interface. The bound RNA is bent, and its distortion may constitute the first step towards RNA unwinding. To dissect the role of the conformational change in the helicase core for RNA unwinding, we characterized the RNA-stimulated ATPase activity, RNA...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Amino Acid Motifs
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DEAD-box RNA Helicases

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to RNA, Bacterial

Source

Open in PubMed Open full text

Identifiers

PMID: 19474341
DOI: 10.1093/nar/gkp397
PMCID: PMC2715247

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN.PMID 19474341Read ↗

Motif III in superfamily 2 "helicases" helps convert the binding energy of ATP into a high-affinity RNA binding site in the yeast DEAD-box protein Ded1.Semantic proximity Read ↗

A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins.Semantic proximity Read ↗

Unwinding the mechanisms of a DEAD-box RNA helicase in cancer.Semantic proximity Read ↗

Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop.Semantic proximity Read ↗

Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.Semantic proximity Read ↗

The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis.Semantic proximity Read ↗

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.Semantic proximity Read ↗

Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera.Semantic proximity Read ↗

Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: role of a highly conserved aromatic-rich sequence.Semantic proximity Read ↗

Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.Semantic proximity Read ↗

Analyses of the functional regions of DEAD-box RNA "helicases" with deletion and chimera constructs tested in vivo and in vitro.Semantic proximity Read ↗

Motifs IV and V in the DEAH box splicing factor Prp22 are important for RNA unwinding, and helicase-defective Prp22 mutants are suppressed by Prp8.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.