PXD051930

PXD051930 is an original dataset announced via ProteomeXchange.

Title	Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus via a direct interaction.
Description	Iron (Fe) is a trace nutrient required by nearly all organisms. As a result of the demand for Fe and the toxicity of non-chelated cytosolic ionic Fe, regulatory systems have evolved to tightly balance Fe acquisition and usage while limiting overload. In most bacteria, including the mammalian pathogen Staphylococcus aureus, the ferric uptake regulator (Fur) is the primary transcriptional regulator that controls the transcription of genes that code for Fe uptake and utilization proteins. Fpa (formaly YlaN) was demonstrated to be essential in Bacillus subtilis unless excess Fe is added to the growth medium, suggesting a role in Fe homeostasis. Here, we demonstrate that Fpa is expendable in S. aureus; however, Fpa became essential upon Fe deprivation. A null fur allele bypassed the essentiality of Fpa. The absence of Fpa nearly abolished the derepression of Fur-dependent transcription during Fe limitation. Bioinformatic analyses suggest that fpa was recruited to Gram positive bacteria and once acquired was maintained in the genome as it co-evolved with Fur. Consistent with a role for Fpa in influencing Fur-dependent regulation, Fpa and Fur interacted in vivo and Fpa inhibits the DNA binding ability of Fur in vitro. Fpa bound Fe(II) in vitro using oxygen or nitrogen ligands with an association constant that is consistent with a physiological role in Fe sensing and/or buffering. These findings have led to a model wherein Fpa is an Fe(II) binding protein that influences Fur-dependent regulation through direct interaction.
HostingRepository	PRIDE
AnnounceDate	2025-05-06
AnnouncementXML	Submission_2025-05-06_15:34:34.439.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Emilee Mustor
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-05-01 13:41:08	ID requested
⏵ 1	2025-05-06 15:34:35	announced

10.1128/mbio.02310-24;

Boyd JM, Ryan Kaler K, Esquil, í, n-Lebr, ó, n K, Pall A, Campbell CJ, Foley ME, Rios-Delgado G, Mustor EM, Stephens TG, Bovermann H, Greco TM, Cristea IM, Carabetta VJ, Beavers WN, Bhattacharya D, Skaar EP, Shaw LN, Stemmler TL, . mBio, 15(11):e0231024(2024) [pubmed]

submitter keyword: sulfur, Staphylococcus aureus, Fpa,iron, Fur, YlaN

Jeffrey M. Boyd
contact affiliation	Department of Biochemistry and Microbiology, Rutgers, the State University of New Jersey, New Brunswick, NJ, USA.
contact email	jeffboyd@sebs.rutgers.edu
lab head
Emilee Mustor
contact affiliation	University of South Florida
contact email	emileemustor@usf.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD051930
     1. Label: PRIDE project
     2. Name: Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus via a direct interaction.