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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Updated: Jun 27, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Rice Serine Hydroxymethyltransferases: Evolution, Subcellular Localization, Function and Perspectives.

Tian Pan1, Hongmiao Jin1, Chuanhui Zhou1

  • 1The Key Laboratory for Quality Improvement of Agricultural Products of Zhejiang Province, College of Advanced Agricultural Sciences, Zhejiang A&F University, Hangzhou 311300, China.

Plants (Basel, Switzerland)
|April 27, 2024
PubMed
Summary
This summary is machine-generated.

This study comprehensively analyzes rice serine hydroxymethyltransferase (SHMT) genes, revealing a gene loss in monocots and unexpected chloroplast localization for OsSHMT3. These SHMTs may play roles in stress responses.

Keywords:
functionriceserine hydroxymethyltransferase

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Area of Science:

  • Plant molecular biology
  • Gene family analysis
  • Rice genetics

Background:

  • Limited functional research exists for serine hydroxymethyltransferase (SHMT) gene family members in rice.
  • Understanding SHMT function is crucial for plant development and stress response.

Purpose of the Study:

  • To conduct a comprehensive investigation of the rice SHMT gene family.
  • To elucidate the phylogenetic relationships, gene structure, expression patterns, subcellular localization, and protein interactions of OsSHMTs.

Main Methods:

  • Phylogenetic analysis
  • Gene structure and promoter analysis
  • Expression profiling
  • Subcellular localization assays (rice protoplasts)
  • Protein-protein interaction studies (dimerization assays)

Main Results:

  • Identified a gene loss event in chloroplast-localized group IIa SHMTs within monocotyledons.
  • OsSHMT3, initially classified as cytoplasmic, was localized to chloroplasts.
  • All five OsSHMTs form homodimers; OsSHMT3 uniquely dimerizes with other OsSHMTs (except OsSHMT1), suggesting a mobile and collaborative role.
  • Predicted cis-acting elements and expression data indicate OsSHMT family involvement in stress and hormone regulation.

Conclusions:

  • OsSHMT3 exhibits unique localization and dimerization properties, potentially acting as a mobile protein in chloroplasts.
  • The OsSHMT family is implicated in diverse stress responses and hormone signaling pathways in rice.
  • This study provides foundational insights for future research into SHMT functions in plants.