Evidence map›Paper›PMID 26586917›Full record

ArticleThe Journal of biological chemistry2016

The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II.

Marieke J Bloemink, Girish C Melkani, Sanford I Bernstein, Michael A Geeves

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Marieke J BloeminkFrom the School of Biosciences, University of Kent, CT2 7NJ Canterbury, United Kingdom and.
Girish C Melkanithe Department of Biology, Molecular Biology Institute, and SDSU Heart Institute at San Diego State University, San Diego, California 92182-4614.
Sanford I Bernsteinthe Department of Biology, Molecular Biology Institute, and SDSU Heart Institute at San Diego State University, San Diego, California 92182-4614. Electronic address: sbernstein@mail.sdsu.edu.
Michael A GeevesFrom the School of Biosciences, University of Kent, CT2 7NJ Canterbury, United Kingdom and. Electronic address: m.a.geeves@kent.ac.uk.
San Diego State University · USUniversity of Kent · GB

Funding

Genetics and Molecular Biology of Striated Muscle MyosinR01GM032443 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI BERNSTEIN, SANFORD I · 1985 to 2016
$6.4M
NIGMS NIH HHS GM32443NIGMS NIH HHS R01 GM032443Wellcome Trust 085309
6 · The paper itself

Abstract

The interface between relay and converter domain of muscle myosin is critical for optimal myosin performance. Using Drosophila melanogaster indirect flight muscle S1, we performed a kinetic analysis of the effect of mutations in the converter and relay domain. Introduction of a mutation (R759E) in the converter domain inhibits the steady-state ATPase of myosin S1, whereas an additional mutation in the relay domain (N509K) is able to restore the ATPase toward wild-type values. The R759E S1 construct showed little effect on most steps of the actomyosin ATPase cycle. The exception was a 25-30% reduction in the rate constant of the hydrolysis step, the step coupled to the cross-bridge recovery stroke that involves a change in conformation at the relay/converter domain interface. Significantly, the double mutant restored the hydrolysis step to values similar to the wild-type myosin. Modeling the relay/converter interface suggests a possible interaction between converter residue 759 and relay residue 509 in the actin-detached conformation, which is lost in R759E but is restored in N509K/R759E. This detailed kinetic analysis of Drosophila myosin carrying the R759E mutation shows that the interface between the relay loop and converter domain is important for fine-tuning myosin kinetics, in particular ATP binding and hydrolysis.

Indexed as

ActinsAdenosine TriphosphatasesAdenosine TriphosphateAnimalsDrosophila melanogasterDrosophila ProteinsHydrolysisKineticsMutation, MissenseProtein Structure, TertiarySkeletal Muscle MyosinsActinsAdenosine TriphosphatasesAdenosine TriphosphateDrosophila ProteinsSkeletal Muscle Myosinsactinfluorescencehomology modelingkineticsmusclemyosinprotein structure-functionsequence alignment

Identifiers

PMID26586917
PMCPMC4722456
OpenAlexW2239037442

What OpenQuestion holds

Textmetadata
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.