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PRMT7 Interacts with ASS1 and Citrullinemia Mutations Disrupt the Interaction
Mamta Verma1, Ramya Chandar M Charles2, Baskar Chakrapani1
1Department of Biotechnology, Pondicherry University, Puducherry 605 014, India.
Journal of Molecular Biology
|June 8, 2017
Summary
Protein arginine methyltransferase 7 (PRMT7) interacts with argininosuccinate synthetase (ASS1). Mutations in ASS1 linked to citrullinemia disrupt this interaction, potentially explaining disease mechanisms.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Protein arginine methyltransferase 7 (PRMT7) regulates gene expression, splicing, DNA damage, and cancer.
- The interaction partners and functions of PRMT7 are not well understood.
Purpose of the Study:
- To identify novel interaction partners of PRMT7.
- To investigate the functional consequences of PRMT7-interacting protein mutations.
Main Methods:
- Yeast two-hybrid screening to identify PRMT7 interactors.
- Pull-down assays to confirm direct interactions.
- Computational modeling to map the interaction interface.
- Site-directed mutagenesis and evolutionary analysis to validate the interface and co-evolution.
Main Results:
- Argininosuccinate synthetase (ASS1) was identified as a PRMT7 interaction partner.
- PRMT7 directly binds to ASS1.
- The interaction interface was mapped and validated in vivo.
- Mutations in ASS1 associated with type I citrullinemia disrupt the PRMT7-ASS1 interaction.
Conclusions:
- PRMT7 directly interacts with ASS1.
- The disruption of the PRMT7-ASS1 interaction by disease-linked mutations provides insight into the molecular pathogenesis of type I citrullinemia.
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