MétaCan
Menu
Back to cohort
Record W2082997720 · doi:10.1074/jbc.m113.491076

Structural Analysis of a Calmodulin Variant from Rice

2013· article· en· W2082997720 on OpenAlexaff
Mostafa Jamshidiha, Hiroaki Ishida, Cindy Sutherland, Jessica L. Gifford, Michael P. Walsh, Hans J. Vogel

Bibliographic record

VenueJournal of Biological Chemistry · 2013
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicPlant Gene Expression Analysis
Canadian institutionsUniversity of Calgary
Fundersnot available
KeywordsCalmodulinLinkerNuclear localization sequencePrenylationCytosolBiophysicsNuclear transportNuclear magnetic resonance spectroscopyC-terminusProtein structureChemistryStereochemistryBiochemistryBiologyNucleusCell biologyAmino acidCell nucleus

Abstract

fetched live from OpenAlex

OsCaM61 is one of five calmodulins known to be present in Oryza sativa that relays the increase of cytosolic [Ca 2+ ] to downstream targets. OsCaM61 bears a unique C-terminal extension with a prenylation site. Using nuclear magnetic resonance (NMR) spectroscopy we studied the behavior of the calmodulin (CaM) domain and the C-terminal extension of OsCaM61 in the absence and presence of Ca 2+ . NMR dynamics data for OsCaM61 indicate that the two lobes of the CaM domain act together unlike the independent behavior of the lobes seen in mammalian CaM and soybean CaM4. Also, data demonstrate that the positively charged nuclear localization signal region in the tail in apo-OsCaM61 is helical, whereas it becomes flexible in the Ca 2+ -saturated protein. The extra helix in apo-OsCaM61 provides additional interactions in the C-lobe and increases the structural stability of the closed apo conformation. This leads to a decrease in the Ca 2+ binding affinity of EF-hands III and IV in OsCaM61. In Ca 2+ -OsCaM61, the basic nuclear localization signal cluster adopts an extended conformation, exposing the C-terminal extension for prenylation or enabling OsCaM61 to be transferred to the nucleus. Moreover, Ser 172 and Ala 173 , residues in the tail, interact with different regions of the protein. These interactions affect the ability of OsCaM61 to activate different target proteins. Altogether, our data show that the tail is not simply a linker between the prenyl group and the protein but that it also provides a new regulatory mechanism that some plants have developed to fine-tune Ca 2+ signaling events. Background: OsCaM61 is a plant CaM bearing a C-terminal extension and a prenylation motif. Results: The C-terminal extension is partially helical and interacts with the CaM domain. Conclusion: OsCaM61 uses the C-terminal extension to control its localization and enzyme activation ability. Significance: This work provides structural details for a new plant regulatory mechanism.

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: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.030
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
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0010.000

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 head0.013
GPT teacher head0.243
Teacher spread0.230 · 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

Citations4
Published2013
Admission routes1
Has abstractyes

Explore more

Same venueJournal of Biological ChemistrySame topicPlant Gene Expression AnalysisFrench-language works237,207