Journal article
Native mass spectrometry identifies an alternative DNA-binding pathway for BirA from Staphylococcus aureus
J Satiaputra, LM Sternicki, AJ Hayes, TL Pukala, GW Booker, KE Shearwin, SW Polyak
Scientific Reports | NATURE PORTFOLIO | Published : 2019
Open access
Abstract
An adequate supply of biotin is vital for the survival and pathogenesis of Staphylococcus aureus. The key protein responsible for maintaining biotin homeostasis in bacteria is the biotin retention protein A (BirA, also known as biotin protein ligase). BirA is a bi-functional protein that serves both as a ligase to catalyse the biotinylation of important metabolic enzymes, as well as a transcriptional repressor that regulates biotin biosynthesis, biotin transport and fatty acid elongation. The mechanism of BirA regulated transcription has been extensively characterized in Escherichia coli, but less so in other bacteria. Biotin-induced homodimerization of E. coli BirA (EcBirA) is a necessary p..
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Awarded by London Mathematical Society
Funding Acknowledgements
We thank the National BioResource Project (NIG, Japan) for the provision of bacterial strains. We would like to thank Dr. Ian Dodd and Dr. Andrew Hao for their assistance and useful discussions, as well as Mr. James Merritt and Ms. Jade Foeng for their assistance with assays. This work was supported by the National Health and Medical Research Council of Australia [Project Grant APP1068885 to SWP and GWB], and the Australian Research Council [Discovery Project DP160101450 to KES]. We are also grateful to the Wallace and Carthew families for their financial support. JS was the recipient of a University of Adelaide Faculty Divisional Scholarship, LMS was the recipient of an Australian Postgraduate Award and AJH was the recipient of a University of Adelaide Scholarship.