Paper · 2020 · Nature Communications

A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin

Sayaka Takehara; Shun Sakuraba; Bunzo Mikami; et al.

6
claims
7
verbatim quotes
51
citations
1
research areas
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Open access · cc-by

Abstract

Abstract Allosteric regulation is protein activation by effector binding at a site other than the active site. Here, we show via X-ray structural analysis of gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO), that such a mechanism maintains hormonal homeostasis in plants. Both enzymes form multimers by interacting via GA 4 and indole-3-acetic acid (IAA) at their binding interface. Via further functional analyses we reveal that multimerization of these enzymes gradually proceeds with increasing GA 4 and IAA concentrations; multimerized enzymes have higher specific activities than monomer forms, a system that should favour the maintenance of homeostasis for these phytohormones. Molecular dynamic analysis suggests a possible mechanism underlying increased GA2ox3 activity by multimerization—GA 4 in the interface of oligomerized GA2ox3s may be able to enter the active site with a low energy barrier. In summary, homeostatic systems for maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently.

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Claims 6

Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

X-ray structural analysis of GA2ox3 and DAO indicates that an allosteric mechanism maintains hormonal homeostasis in plants.

Taxon
plantsViridiplantaee0
Gene
gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO)e0
Outcome
hormonal homeostasise0

Verbatim

e0

“we show via X-ray structural analysis of gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO), that such a mechanism maintains hormonal homeostasis in plants”

✓ located verbatim in the source · abstract, characters 117–283 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

Both enzymes form multimers through interaction via GA4 and indole-3-acetic acid (IAA) at their binding interface.

Compound
GA 4 and indole-3-acetic acid (IAA)e0
Outcome
form multimerse0

Not reportedTaxonDirection

Verbatim

e0

“Both enzymes form multimers by interacting via GA 4 and indole-3-acetic acid (IAA) at their binding interface”

✓ located verbatim in the source · abstract, characters 285–394 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

Multimerization of the enzymes proceeds gradually with increasing GA4 and IAA concentrations.

Compound
GA 4 and IAAe0
Outcome
multimerization of these enzymese0
Direction
increaseinferrede0

Not reportedTaxon

Verbatim

e0

“multimerization of these enzymes gradually proceeds with increasing GA 4 and IAA concentrations”

✓ located verbatim in the source · abstract, characters 443–538 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

Multimerized enzymes have higher specific activities than monomer forms.

Outcome
specific activitiese0
Direction
highere0
Comparator
monomer formse0

Not reportedTaxon

Verbatim

e0

“multimerized enzymes have higher specific activities than monomer forms”

✓ located verbatim in the source · abstract, characters 540–611 · show in text ↑
Mechanismhypothesisoriginal resultsimulated

Claim · model-written summary

Molecular dynamic analysis suggests that GA4 in the interface of oligomerized GA2ox3 may enter the active site with a low energy barrier, a possible mechanism for increased GA2ox3 activity by multimerization.

Gene
GA2ox3e0
Compound
GA 4e1
Outcome
increased GA2ox3 activity by multimerizatione0

Not reportedTaxon

Verbatim

e0

“Molecular dynamic analysis suggests a possible mechanism underlying increased GA2ox3 activity by multimerization”

✓ located verbatim in the source · abstract, characters 697–809 · show in text ↑
e1

“GA 4 in the interface of oligomerized GA2ox3s may be able to enter the active site with a low energy barrier”

✓ located verbatim in the source · abstract, characters 810–918 · show in text ↑
Mechanismhypothesisoriginal resultbasis n/a

Claim · model-written summary

Homeostatic systems maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently.

Compound
GA and IAAe0
Outcome
homeostatic systems for maintaining GA and IAA levelse0
Qualifier
appear to have developed independentlye0

Not reportedTaxon

Verbatim

e0

“homeostatic systems for maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently”

✓ located verbatim in the source · abstract, characters 932–1065 · show in text ↑