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The Application of Differential Scanning Fluorimetry in Exploring Bisubstrate Binding to Protein Arginine <i>N</i> ‐Methyltransferase 1

2021· article· en· W3166979465 on OpenAlexafffund
Jennifer I. Brown, Brent D. G. Page, Adam Frankel

Bibliographic record

VenueThe FASEB Journal · 2021
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicCancer-related gene regulation
Canadian institutionsUniversity of British Columbia
FundersNatural Sciences and Engineering Research Council of CanadaMichael Smith Health Research BC
KeywordsCofactorChemistryPeptideEnzymeActive siteLigand (biochemistry)StereochemistryBinding siteBiochemistryBiophysicsReceptorBiology

Abstract

fetched live from OpenAlex

Background Protein arginine N ‐methyltransferases (PRMTs) methylate polypeptide substrates using a methyl‐donor cofactor S ‐adenosyl‐L‐methionine (SAM). The binding mechanisms of both the cofactor and target substrates have been explored using transient and steady‐state kinetic experiments. However, many of these studies have found conflicting results due to the difficult and sometimes subjective interpretation of kinetic data. Therefore, a robust understanding of the PRMT bisubstrate mechanism can only be achieved through use of complementary structural and biophysical techniques. We hypothesize that thermal shift assays, which are widely used to monitor ligand‐receptor interactions in drug discovery processes, may be applied in a novel way to reveal order of bisubstrate binding to PRMTs. Methods We used differential scanning fluorimetry (DSF) to measure protein melting temperature ( T m ) changes in response to ligand binding. Protein unfolding was monitored using an environmentally sensitive dye SYPRO™ Orange, whose fluorescence increases when exposed to hydrophobic patches of unfolded protein. Cofactor analogues, peptide substrates, and an active site inhibitor were incubated with human PRMT1 to observe their individual and combined effects on enzyme stability; ligands which result in a higher T m interact with and stabilize the enzyme. Results We found that the cofactor analogues induce a positive shift in T m , indicating a stabilizing effect on PRMT1. Conversely, peptide substrates do not stabilize the enzyme and instead lead to a destabilizing, negative shift in T m . Together though, both cofactor and peptide substrate have an additive stabilizing effect on PRMT1. We also found that the active site inhibitor only interacts with PRMT1 in the presence of cofactor and causes a significant positive and stabilizing thermal shift. Conclusions We demonstrate for the first time that DSF can be used to explore the order of substrate binding to enzymes. Our results corroborate other structural, biophysical, and kinetic data which demonstrate that cofactor binding must precede target substrate binding for catalysis to occur. The enzyme:cofactor:substrate complex forms a stable structure that is conducive to methyl transfer. This technique is a valuable complement to kinetic experiments that will contribute to a sound understanding of enzyme kinetic mechanisms.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.001
metaresearch head score (Gemma)0.001
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.005

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0010.001
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0010.001
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.018
GPT teacher head0.254
Teacher spread0.236 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

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Citations0
Published2021
Admission routes2
Has abstractyes

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