Characterization of Arabidopsis π/π hydrolase mutants involved in PAA degradation
Faculty Mentor
Marylou Chitiyo
Location
Savannah Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Biology
Abstract
Polyaspartic acid (PAA) is a biodegradable polymer with many industrial applications, and is thermally synthesized from the naturally occurring aspartic acid. PAA is widely used in crop production to enhance plant growth and yield. Bacterial enzymes PahZ1KT-1, PahZ2KT-1 from Sphingomonas and PahZ1KP-2 from Pedobacter belonging to the π/π hydrolase superfamily are implicated in the sequential degradation of PAA to aspartate, a key metabolite for plant growth. It is known that plants release root extracellular enzymes, including hydrolases. However, it is not established whether in the absence of bacteria, plants can degrade PAA. The objective of this study is to characterize Arabidopsis mutants impaired in selected hydrolase genes to identify those with potential to degrade PAA. We conducted bioinformatics analyses and identified enzymes in Arabidopsis thaliana that are homologous to PahZ1 and PahZ2. Bioinformatics analyses of Arabidopsis and bacterial hydrolases revealed sequence identities ranging from 11-61% (PahZ1) and 18-20% (PahZ2). We obtained Arabidopsis mutant seeds and grew plants in agar-based media. Results show mutant specific differences in root length and root hair development in response to PAA. We observed delayed germination in one mutant. We have identified mutants with impaired or interesting responses to PAA and are conducting protein expression analyses in E. coli.
Program Description
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Start Date
4-21-2026 10:00 AM
End Date
4-21-2026 12:00 PM
Recommended Citation
Lundy, Anne, "Characterization of Arabidopsis π/π hydrolase mutants involved in PAA degradation" (2026). GS4 Student Scholars Symposium. 24.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026A/2026A/24
Characterization of Arabidopsis π/π hydrolase mutants involved in PAA degradation
Savannah Ballroom
Polyaspartic acid (PAA) is a biodegradable polymer with many industrial applications, and is thermally synthesized from the naturally occurring aspartic acid. PAA is widely used in crop production to enhance plant growth and yield. Bacterial enzymes PahZ1KT-1, PahZ2KT-1 from Sphingomonas and PahZ1KP-2 from Pedobacter belonging to the π/π hydrolase superfamily are implicated in the sequential degradation of PAA to aspartate, a key metabolite for plant growth. It is known that plants release root extracellular enzymes, including hydrolases. However, it is not established whether in the absence of bacteria, plants can degrade PAA. The objective of this study is to characterize Arabidopsis mutants impaired in selected hydrolase genes to identify those with potential to degrade PAA. We conducted bioinformatics analyses and identified enzymes in Arabidopsis thaliana that are homologous to PahZ1 and PahZ2. Bioinformatics analyses of Arabidopsis and bacterial hydrolases revealed sequence identities ranging from 11-61% (PahZ1) and 18-20% (PahZ2). We obtained Arabidopsis mutant seeds and grew plants in agar-based media. Results show mutant specific differences in root length and root hair development in response to PAA. We observed delayed germination in one mutant. We have identified mutants with impaired or interesting responses to PAA and are conducting protein expression analyses in E. coli.
