# Sequence Variation and In Silico Protein Characterization of γ-TMT Gene in Mutant Rodent Tuber (Typhonium flagelliforme Lodd.)

**Authors:** Nesti Fronika Sianipar, Zidni Muflikhati, Reflinur, Muhammad Dylan Lawrie, Dave Mangindaan, Khoirunnisa Assidqi, Chukwunwike Uchenna Enyi, Dwiyantari Widyaningrum

PMC · DOI: 10.3390/ijms26157148 · International Journal of Molecular Sciences · 2025-07-24

## TL;DR

This study examines the γ-TMT gene in a mutant plant to understand how genetic changes affect protein structure and antioxidant production.

## Contribution

The study identifies sequence and structural variations in the γ-TMT gene of a mutant plant, linking them to potential changes in tocopherol biosynthesis.

## Key findings

- The γ-TMT gene in mutant plants shows base substitutions and deletions compared to wild-type plants.
- Predicted protein structures show differences in helix and loop orientation, especially in the C-terminal domain.
- Structural changes suggest possible links to increased tocopherol biosynthesis, though experimental validation is needed.

## Abstract

γ-tocopherol is an important antioxidant compound associated with anticancer activity in several plants. This study aimed to analyze the γ-TMT (γ-tocopherol methyltransferase) gene sequence and predict its protein structure in mutant rodent tuber (Typhonium flagelliforme Lodd.) plants. Degenerate primers were designed from homologous sequences in monocot species and used to amplify the γ-TMT gene. Amplification of the γ-TMT gene was observedin the mutant and the wild-type plants. The amplified region partially covers the γ-TMT gene, which has undergone mutations due to a combination of somaclonal variation and gamma irradiation. Sequence analysis revealed notable variations between mutant and wild-type lines, including base substitutions and deletions. Predicted protein structures based on the coding DNA sequence (CDS) revealed notable differences in helix and loop orientation, particularly in the C-terminal domain and central regions of the protein. These structural differences suggest potential links to increased tocopherol biosynthesis or biological activity; however, further experimental validation is required to confirm these functional implications. This study provides foundational insights into the link between the expression of the γ-TMT gene and tocopherol biosynthesis and supports the development of specific molecular markers in T. flagelliforme.

## Linked entities

- **Genes:** G-TMT (gamma-tocopherol methyltransferase) [NCBI Gene 842805]
- **Proteins:** G-TMT (gamma-tocopherol methyltransferase)

## Full-text entities

- **Chemicals:** tocopherol (MESH:D024505), gamma-tocopherol (MESH:D024504)
- **Species:** Typhonium flagelliforme (species) [taxon 458697], Rodentia (rodent, order) [taxon 9989]

## Full text

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## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12346533/full.md

## References

41 references — full list in the complete paper: https://tomesphere.com/paper/PMC12346533/full.md

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Source: https://tomesphere.com/paper/PMC12346533