Evidence map›Paper›PMID 18165229›Full record

ArticleThe Journal of biological chemistry2008

Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase.

Jonathan A R Worrall, Françoise S Howe, Adam R McKay, Carol V Robinson, Ben F Luisi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. The RNA degradosome promotes tRNA quality control through clearance of hypomodified tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  14. The Q motif of a viral packaging motor governs its force generation and communicates ATP recognition to DNA interaction.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 2 countries.

Jonathan A R WorrallDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA.
Françoise S Howe
Adam R McKay
Carol V Robinson
Ben F Luisi
University of Cambridge · GB

Funding

Wellcome Trust 042079
6 · The paper itself

Abstract

Helicase B (RhlB) is one of the five DEAD box RNA-dependent ATPases found in Escherichia coli. Unique among these enzymes, RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities. To explore the basis for this activating effect, we have generated a di-cistronic vector that overexpresses a complex comprising RhlB and its recognition site within RNase E, corresponding to residues 696-762. Complex formation has been characterized by isothermal titration calorimetry, revealing an avid, enthalpy-favored interaction between the helicase and RNase E-(696-762) with an equilibrium binding constant (Ka) of at least 1 x 10(8) m(-1). We studied ATPase activity of mutants with substitutions within the ATP binding pocket of RhlB and on the putative interaction surface that mediates recognition of RNase E. For comparisons, corresponding mutations were prepared in two other E. coli DEAD box ATPases, RhlE and SrmB. Strikingly, substitutions at a phenylalanine near the Q-motif found in DEAD box proteins boosts the ATPase activity of RhlB in the absence of RNA, but completely inhibits it in its presence. The data support the proposal that the protein-protein and RNA-binding surfaces both communicate allosterically with the ATPase catalytic center. We conjecture that this communication may govern the mechanical power and efficiency of the helicases, and is tuned in individual helicases in accordance with cellular function.

Indexed as

Adenosine TriphosphatasesAllosteric RegulationAmino Acid MotifsAmino Acid SubstitutionBinding SitesDEAD-box RNA HelicasesEndoribonucleasesEscherichia coliEscherichia coli ProteinsMultiprotein ComplexesMutation, MissenseProtein BindingProtein Structure, QuaternaryRNA, BacterialAdenosine TriphosphatasesDEAD-box RNA HelicasesEndoribonucleasesEscherichia coli ProteinsMultiprotein Complexesribonuclease ERNA, Bacterial

Identifiers

PMID18165229
PMCPMC7611231
OpenAlexW2056431229

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.