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Structural and functional roles for β‐strand 7 in the α‐crystallin domain of p26, a polydisperse small heat shock protein from <i>Artemia franciscana</i>

2006· article· en· W2078020789 on OpenAlexaff
Yu Sun, Svetla Bojikova‐Fournier, Thomas H. MacRae

Bibliographic record

VenueFEBS Journal · 2006
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicHeat shock proteins research
Canadian institutionsDalhousie University
Fundersnot available
KeywordsBiologyDimerHeat shock proteinCell biologyBiophysicsChaperone (clinical)Amino acidBiochemistryChemistryGene

Abstract

fetched live from OpenAlex

Oviparous development in the extremophile crustacean, Artemia franciscana, generates encysted embryos which enter a profound state of dormancy, termed diapause. Encystment is marked by the synthesis of p26, a polydisperse small heat shock protein thought to protect embryos from stress. In order to elucidate structural/functional relationships within p26 and other polydisperse small heat shock proteins, and to better define the protein's role during diapause, amino acid substitutions R110G, F112R, R114A and Y116D were generated within the p26 alpha-crystallin domain by site-directed mutagenesis. These residues were chosen because they are highly conserved across species boundaries, and molecular modelling indicates that they are part of a key structural interface between dimers. The F112R mutation, which had the greatest impact on oligomerization, placed two charged residues at the p26 dimer-dimer interface, demonstrating the importance of beta-strand 7 in tetramer formation. All mutated versions of p26 were less able than wild-type p26 to confer thermotolerance on transformed bacteria and they exhibited diminished chaperone action in three in vitro assays; however, all variants retained protective activity. This apparent stability of p26 may, by prolonging effective chaperone life in vivo, enhance embryo stress resistance. All substitutions modified p26 intrinsic fluorescence, surface hydrophobicity and secondary structure, and the pronounced changes in variant R114A, as indicated by these physical measurements, correlated with the greatest loss of function. Although mutation R114A had the greatest effect on p26 chaperoning, it had the least on oligomerization. These results demonstrate that in contrast to many other small heat shock proteins, p26 effectiveness as a chaperone is independent of oligomerization. The results also reinforce the idea, occasioned by modelling, that R114 is removed slightly from dimer-dimer interfaces. Moreover, beta-strand 7 is shown to have an important role in oligomerization of p26, a function first proposed for this structural element upon crystallization of wheat Hsp16.9, a small heat shock protein with different quaternary structure.

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 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 score0.230
Threshold uncertainty score0.415

Codex and Gemma teacher scores by category

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

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 head0.012
GPT teacher head0.240
Teacher spread0.228 · 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.

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".

Quick stats

Citations25
Published2006
Admission routes1
Has abstractyes

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