Journal article
An investigation into the effect of ribosomal protein S15 phosphorylation on its intermolecular interactions by using phosphomimetic mutant
D Correddu, N Sharma, S Kaur, KG Varnava, NM Mbenza, V Sarojini, IKH Leung
Chemical Communications | ROYAL SOC CHEMISTRY | Published : 2020
DOI: 10.1039/d0cc01618g
Abstract
An investigation using recombinant ribosomal proteins and synthetic peptide models was conducted to uncover the effect of the introduction of a negative charge at the C-terminal tail of ribosomal protein S15. Our results help provide a chemical rationale towards understanding how G2019S LRRK2, a common clinical mutation, causes Parkinson's disease.
Grants
Funding Acknowledgements
We thank the Health Research Council of New Zealand (Emerging Researcher First Grant), Neurological Foundation of New Zealand (Small Project Grant), Biochemical Society (Eric Reid Fund for Methodology) and the University of Auckland (Faculty Research Development Fund - New Staff Research Fund) for funding. D. C. was supported by a doctoral scholarship underwritten by the School of Chemical Sciences, The University of Auckland. We thank Dr Angus C. Grey (The University of Auckland) for technical support for MALDI mass spectrometry, Dr Bincy Jacob and Martin J. Middleditch (The University of Auckland) for protein gel band mass spectrometry analyses, and Dr Michael Schmitz (The University of Auckland) for maintenance of the NMR spectroscopy facility. We thank Dr Ries J. Langley for providing the vector pGEX-2T.