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Record W2911273999 · doi:10.1107/s0108767318096423

Structural and functional analysis of yeast Shu complex

2018· article· en· W2911273999 on OpenAlexaff
Sam Chu

Bibliographic record

VenueActa Crystallographica Section A Foundations and Advances · 2018
Typearticle
Languageen
FieldMaterials Science
TopicLanthanide and Transition Metal Complexes
Canadian institutionsWestern University
Fundersnot available
KeywordsYeastComputational biologyFunctional analysisChemistryBiologyBiochemistryGene

Abstract

fetched live from OpenAlex

The error-free DNA lesion bypass pathway is a DNA damage tolerance response that switches replication templates with homologous recombination (HR) to fix DNA damage and ensure genomic authenticity. The spatial and temporal arrangement of proteins in the error-free lesion bypass pathway is largely undefined. The budding yeast Shu complex has been discovered to be crucial for DNA binding and other activities in the HR apparatus. The Shu complex structure has been determined and some key proteins of the error-free lesion bypass pathway have been identified. The molecular basis in which these proteins are organized remains unclear. We are working to characterize the structure and function of the Shu complex interacting with substrates through X-ray crystallography and related functional assays. The binding of specific DNA substrates would cause a conformational change to the Shu complex, which affects its ability to hydrolyze ATP. Structural data will help provide insights into the mechanism of the Shu complex and how it promotes the error-free bypass pathway at the molecular level. DNA substrates with different lengths and end natures were assayed via gel mobility shift and fluorescence polarization/anisotropy to identify substrates that interact best with the Shu complex. Preliminary data generated from malachite green ATPase assays suggest the Shu complex possess ATPase activity that is DNA-binding dependent. Thus far, crystals of the Csm2-Psy3 dimer in complex with DNA diffracted to a resolution of 2.8 in the space group of P312, which was different from the apo dimer's C2 space group. It is unclear if the DNA binding influenced the protein's structure without additional evidence from a structure with improved resolution. Additionally, crystals generated from Shu complex incubated with ATP and AMP-PNP diffracted in the same P43212 space group as the published Shu complex structure. Optimization of the crystallization condition for higher quality data is necessary to confirm the presence/absence of the substrates. In summary, structure built from the DNA-protein complex data could not confirm the DNA substrate relative to the Csm2-Psy3 dimer. Despite the ability to generate crystals, the substrate may not be the most suitable for the complex to consistently occupy a space in the structure. Optimization for better diffraction quality crystals of the Shu complex with ATP/AMP-PNP is underway. Conclusions drawn from this research will lay the foundation for understanding the mechanism of the error-free DNA damage tolerance to aid in combating various diseases like cancers and genetic defects.

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 distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesInsufficient payload (model declined to judge)
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: none
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.988
Threshold uncertainty score1.000

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.001
Science and technology studies0.0000.001
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
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 head0.027
GPT teacher head0.272
Teacher spread0.245 · 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 teacher head, not a consensus.

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".

Quick stats

Citations0
Published2018
Admission routes1
Has abstractyes

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