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Tuning a timing device that regulates lateral root development in rice.

Lucila Andrea Acevedo1,2, Nathan E Korson1, Justin M Williams1

  • 1Department of Molecular Biology & Genetics, Cornell University, Ithaca, NY, 14853, USA.

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|August 14, 2019
PubMed
Summary

Rice Peptidyl Prolyl Isomerase (PPIase) LRT2 is key for lateral root growth. Mutants were characterized to understand its role in auxin signaling and root development, revealing stable variants with altered isomerization activity.

Keywords:
Auxin circuitCis–trans isomerizationExchange kineticsLRT2LRT2 mutationsOsIAA11

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Area of Science:

  • Plant molecular biology
  • Biochemistry
  • Developmental biology

Background:

  • Peptidyl Prolyl Isomerases (PPIases) catalyze cis-trans isomerization of prolyl peptide bonds, a critical step in protein function.
  • In rice, the PPIase LRT2 is essential for lateral root initiation and development.
  • LRT2 acts on the OsIAA11 substrate, influencing auxin signaling and degradation pathways.

Purpose of the Study:

  • To characterize the thermal stability and isomerization rates of wild-type (WT) LRT2 and its mutants.
  • To investigate the impact of specific mutations on LRT2's interaction with its substrate OsIAA11.
  • To compare the activity of rice LRT2 with homologs from other species.

Main Methods:

  • Site-directed mutagenesis of the LRT2 gene.
  • In vitro assays to measure isomerization rates and thermal stability of LRT2 variants.
  • Biochemical characterization of LRT2 homologs (hCypA, TaCypA, PPIB) using the OsIAA11 substrate.

Main Results:

  • Several thermally stable LRT2 mutants were identified, including P125K, W128A, and H133Q, exhibiting reduced catalytic activity compared to WT.
  • Mutations affected substrate binding and catalytic competence.
  • Homologs hCypA, TaCypA, and PPIB showed varying levels of activity on the OsIAA11 substrate.

Conclusions:

  • Characterized LRT2 mutants provide valuable tools for studying the dynamics of the auxin circuit and lateral root development.
  • Understanding LRT2's enzymatic activity and stability is crucial for dissecting its role in plant hormone signaling.
  • Comparative analysis with homologs deepens insights into PPIase function across species.