PMT2

UniProt ID: Q93XQ4
Organism: Nicotiana attenuata
Review Status: DRAFT
Aliases:
NaPMT1.2 NaPMT2 Putrescine N-methyltransferase 2
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Gene Description

PMT2 is a root-expressed putrescine N-methyltransferase paralog from Nicotiana attenuata that converts putrescine to N-methylputrescine for the pyrrolidine branch of nicotine biosynthesis. Like PMT1, it is embedded in the inducible nicotine defense program and shows jasmonate-, wound-, and herbivory-responsive transcript accumulation.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003824 catalytic activity
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: This annotation is correct only at a very generic level and should not be treated as an informative curation outcome for PMT2.
Reason: GO:0030750 putrescine N-methyltransferase activity already captures the actual chemistry performed by PMT2.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
PMT catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, the first specific metabolite on the route to nicotine.
GO:0004766 spermidine synthase activity
IEA
GO_REF:0000118
REMOVE
Summary: This TreeGrafter assignment is a family-level miscall and should not be kept as the catalytic function of PMT2.
Reason: PMT2 belongs to a lineage derived from spermidine synthase but now performs specialized methyltransferase chemistry in nicotine biosynthesis.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
TreeGrafter assignment to spermidine synthase reflects PMT's evolutionary origin from spermidine synthase rather than its present catalytic activity.
GO:0005829 cytosol
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: Cytosolic localization is plausible for PMT2 but is not a major focus of the current literature-backed curation pass.
Reason: Retain the localization as a reasonable non-core inference while prioritizing the better-supported catalytic and pathway assignments.
GO:0008295 spermidine biosynthetic process
IEA
GO_REF:0000118
REMOVE
Summary: This process annotation does not fit PMT2 biology. PMT2 contributes to nicotine alkaloid production, not spermidine biosynthesis.
Reason: The same family-level overtransfer that caused the spermidine synthase activity annotation also incorrectly projects PMT2 into the spermidine process.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
PMT catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, the first specific metabolite on the route to nicotine.
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
TreeGrafter assignment to spermidine synthase reflects PMT's evolutionary origin from spermidine synthase rather than its present catalytic activity.
GO:0009753 response to jasmonic acid
IEA
GO_REF:0000117
KEEP AS NON CORE
Summary: Jasmonate responsiveness is supported for PMT2, but it is better treated as regulatory context than as a core function.
Reason: MeJA induction is part of the defense program that controls PMT2 expression, yet the core role of the gene is catalytic entry into nicotine biosynthesis.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
In N. attenuata, Winz and Baldwin cloned PMT1 and PMT2 and found that both root PMT transcripts rose after MeJA, wounding, and Manduca sexta herbivory, while ethylene suppressed this induction.
GO:0030750 putrescine N-methyltransferase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the core molecular function of PMT2 and accurately captures the enzyme's specialized chemistry.
Reason: PMT2 catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
PMT catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, the first specific metabolite on the route to nicotine.
GO:0042179 nicotine biosynthetic process
IEA
GO_REF:0000041
ACCEPT
Summary: This is an appropriate core pathway assignment for PMT2.
Reason: PMT2 generates the first dedicated pyrrolidine-branch intermediate and is part of the duplicated root nicotine pathway in N. attenuata.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
PMT catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, the first specific metabolite on the route to nicotine.
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
UniProt curates Q93XQ4 as Putrescine N-methyltransferase 2 and places it in nicotine biosynthesis with predominant root expression.
GO:0009611 response to wounding
IEP
PMID:11299398
Molecular interactions between the specialist herbivore Mand...
KEEP AS NON CORE
Summary: Wound-responsive expression is supported for PMT2 but is ancillary to the gene's catalytic pathway role.
Reason: Retain the annotation as valid defense-response context without elevating it above the core enzymatic curation.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
In N. attenuata, Winz and Baldwin cloned PMT1 and PMT2 and found that both root PMT transcripts rose after MeJA, wounding, and Manduca sexta herbivory, while ethylene suppressed this induction.
GO:0009625 response to insect
IEP
PMID:11299398
Molecular interactions between the specialist herbivore Mand...
KEEP AS NON CORE
Summary: PMT2 participates in insect-triggered defense induction, but that inducibility is not its central curated function.
Reason: Manduca sexta feeding induces PMT transcripts as part of nicotine defense, so the annotation should be preserved as a non-core context term.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
In N. attenuata, Winz and Baldwin cloned PMT1 and PMT2 and found that both root PMT transcripts rose after MeJA, wounding, and Manduca sexta herbivory, while ethylene suppressed this induction.
GO:0009753 response to jasmonic acid
IEP
PMID:11299398
Molecular interactions between the specialist herbivore Mand...
KEEP AS NON CORE
Summary: The experimental annotation is supported, but the response term should remain explicitly non-core in this review.
Reason: MeJA induction helps explain defense regulation of PMT2 without changing the gene's primary biochemical interpretation.
Supporting Evidence:
file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
In N. attenuata, Winz and Baldwin cloned PMT1 and PMT2 and found that both root PMT transcripts rose after MeJA, wounding, and Manduca sexta herbivory, while ethylene suppressed this induction.

Core Functions

PMT2 catalyzes the S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, providing the same committed pyrrolidine-branch entry chemistry as PMT1 within the duplicated Nicotiana attenuata root nicotine pathway.

Supporting Evidence:
  • file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
    PMT catalyzes S-adenosylmethionine-dependent methylation of putrescine to N-methylputrescine, the first specific metabolite on the route to nicotine.
  • file:NICAT/NaPMT1.2/NaPMT1.2-notes.md
    The 2017 Nicotiana genome paper places root nicotine biosynthesis in N. attenuata as a duplicated specialization of polyamine and NAD metabolism, consistent with PMT as a root defense-pathway enzyme.

References

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Suggested Questions for Experts

Q: Are PMT1 and PMT2 dosage balanced in roots, or does one paralog dominate inducible nicotine flux under natural herbivory?

Q: How should PMT3 be classified relative to PMT1 and PMT2 once the core duplicated pathway members are fully reviewed?

Suggested Experiments

Experiment: Measure nicotine-pathway metabolites and transcript compensation in PMT2 single-loss and PMT1 PMT2 double-loss lines before and after methyl jasmonate or Manduca sexta challenge.

Hypothesis: PMT2 contributes nonredundant but overlapping catalytic flux within the inducible root nicotine pathway.

Type: genetic perturbation plus metabolite profiling

Experiment: Reconstitute PMT2 biochemistry in vitro and compare catalytic efficiency and substrate preference directly against PMT1 using the same assay conditions.

Hypothesis: PMT2 retains core PMT chemistry but may differ quantitatively from PMT1 in kinetics or stability.

Type: biochemical enzyme assay

Deep Research

OpenAI

(NaPMT1.2-deep-research-openai.md)

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πŸ“š Additional Documentation

Notes

(NaPMT1.2-notes.md)

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