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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
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Moonlighting proteins: putting the spotlight on enzymes
Sara Abolhassani Rad1, Emily J Clayton1, Emily J Cornelius1
1a Department of Biology , Western University , London , Canada.
Plant Signaling & Behavior
|September 26, 2018
Summary
Arogenate dehydratase 2 (ADT2) in Arabidopsis thaliana has a dual role. Beyond phenylalanine biosynthesis, ADT2 is crucial for chloroplast division, interacting with FtsZ and acting early in the process.
Area of Science:
- Plant Biology
- Molecular Biology
- Cell Biology
Background:
- Arogenate dehydratase 2 (ADT2) is part of the Arabidopsis thaliana ADT family, enzymes involved in phenylalanine biosynthesis.
- ADT2 localizes to chloroplast stromules and forms a ring around dividing chloroplasts, suggesting a non-enzymatic role in plastid division (PD).
Purpose of the Study:
- To provide further evidence for the non-enzymatic role of ADT2 in chloroplast division.
- To investigate the relationship between ADT2 and key chloroplast division proteins, FtsZ, ARC3, ARC5, and ARC6.
Main Methods:
- Co-localization studies of ADT2 and FtsZ using fluorescent proteins.
- Analysis of ADT2 and FtsZ expression in wild-type and mutant Arabidopsis lines (adt2, arc3, arc5, arc6).
Main Results:
- ADT2 and FtsZ were found to co-localize at the equatorial plane of dividing chloroplasts.
- ADT2 expression patterns in arc3 and arc6 mutants mimicked FtsZ misexpression.
- In arc5 mutants, ADT2 ring positioning indicated correct timing relative to constriction.
- ADT2's role in PD precedes ARC5 but depends on ARC3 and ARC6.
Conclusions:
- ADT2 plays a significant, non-enzymatic role in Arabidopsis chloroplast division.
- ADT2 functions in coordination with FtsZ and the ARC proteins, with its activity being upstream of ARC5 and dependent on ARC3 and ARC6.
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