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Cell pellets were resuspended in PBS containing cOmplete EDTA-free Protease Inhibitor Cocktail (Roche) and 1.4 mM diamide (Sigma-Aldrich) and lysed mechanically using a FastPrep-24 (MP Biomedicals). Protein concentration was determined by Bradford assay (Bio-Rad). Trypsin digestion and peptide preparation were performed by the Mass Spectrometry Research Center, Vanderbilt University Medical Center. Peptides were resuspended in 0.2% formic acid at 200 ng/μL and adjusted to 50 ng/μL prior to acquisition. 0.015% n-dodecyl-β-d-maltoside was added prior to diaPASEF acquisition. 150 ng of peptides were separated on a C18 reverse-phase column (100 μm × 20 cm, 3 μm Jupiter, Phenomenex) via a 30-min gradient on a nanoELUTE2 and analyzed on a timsTOF HT instrument (Bruker); data were collected across 12 PASEF ramps (0.75–1.3 1/k0, 350–1250 m/z) using variable isolation windows (12.27–122.81 Th, 50 ms accumulation)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw diaPASEF data files were processed using Spectronaut V20 (Biognosys) against the Streptococcus pyogenes MGAS315 proteome (UniProt proteome UP000000564). Protein-level label-free quantification (LFQ) intensities were exported and differential abundance analysis was performed in R (v4.5.3) using the limma package with empirical Bayes variance moderation and Benjamini-Hochberg multiple testing correction."],"omics_type":["Proteomics"],"labhead":["Anthony R. Flores"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Vanderbilt University Medical Center"],"species":["Streptococcus Pyogenes Mgas315"],"publication":["42367948 Morrison GA, Vega LA, Sanson Iglesias M, Holly K, McDonald WH, Horstmann N, Shelburne SA, Gaddy JA, Flores AR. SpxA1 and SpxA2 Function as a Stoichiometry-Dependent Regulatory Rheostat Governing Virulence Gene Expression in Group A Streptococcus. bioRxiv. 2026:2026.06.19.733365 10.64898/2026.06.19.733365"],"submitter_mail":["anthony.flores@vumc.org"],"submitter_affiliation":["Vanderbilt University Medical Center"],"submitter_country":["United States"],"pubmed_abstract":["Group A Streptococcus (GAS) is a human-restricted pathogen whose global incidence has surged in the post-COVID era. The ability of GAS to shift from a colonizing to invasive phenotype depends on coordinated virulence gene regulation in response to host-derived signals. However, the mechanisms by which individual stress-sensing systems interact to reshape the virulence gene regulatory landscape remain incompletely understood. Here we define the regulatory programs of two conserved transcriptional regulator paralogs, SpxA1 and SpxA2, using an integrated multi-omic approach combining RNA-seq, data-independent acquisition proteomics, NanoString-based transcriptional profiling across multiple host-relevant stress conditions, and chromatin immunoprecipitation with exonuclease treatment (ChIP-exo). RNA-seq revealed functionally distinct regulons with SpxA1 governing oxidative stress defense and SpxA2 coordinating virulence-associated gene expression linked to the CovRS two-component regulatory system. Proteomic analysis established SpxA2 as a ClpXP protease substrate in GAS and identified reciprocal paralog accumulation upon loss of either SpxA1 or SpxA2, consistent with compensatory transcriptional upregulation. NanoString profiling under bacitracin and human neutrophil peptide-1 challenge identified four gene modules with distinct stoichiometry-dependent and condition-dependent regulatory logic, revealing that the SpxA1/SpxA2 ratio rather than the activity of either paralog alone determines which transcriptional programs are engaged. ChIP-exo demonstrated that SpxA2 directly modulates CovR-DNA binding occupancy in a CovR binding motif-dependent manner, simultaneously antagonizing CovR dimer binding at an extended (25-bp) CovR motif and facilitating CovR monomer binding at the canonical ATTARA motif. These findings establish the LiaFSR-SpxA2-CovRS axis as a cross-regulatory circuit through which GAS cell envelope stress sensing is directly transduced into coordinated virulence gene regulatory changes."],"pubmed_title":["SpxA1 and SpxA2 Function as a Stoichiometry-Dependent Regulatory Rheostat Governing Virulence Gene Expression in Group A Streptococcus."],"pubmed_authors":["Morrison Gretchen A GA, Vega Luis Alberto LA, Iglesias Misú Sanson MS, Holly Khufu K, McDonald W Hayes WH, Horstmann Nicola N, Shelburne Samuel A SA, Gaddy Jennifer A JA, Flores Anthony R AR"],"additional_accession":[]},"is_claimable":false,"name":"SpxA1 and SpxA2 Function as a Stoichiometry-Dependent Regulatory Rheostat Governing Virulence Gene Expression in Group A Streptococcus — DIA Proteomics","description":"Group A Streptococcus (GAS) encodes two paralogs of the Spx transcriptional regulator, SpxA1 and SpxA2, which interact with RNA polymerase to modulate virulence gene expression. SpxA2 is directly regulated by the LiaFSR three-component system in response to antimicrobial peptide stress. To define how SpxA2 influences CovR DNA occupancy genome-wide, we performed chromatin immunoprecipitation with exonuclease treatment (ChIP-exo) targeting CovR in wild-type MGAS10870 (emm3), an isogenic spxA2 deletion mutant (deltaSpxA2), and a LiaSQ146A constitutively active LiaS mutant used as a SpxA2 overexpression surrogate (SpxA2-OE). Differential binding analysis identified 439 sites with significantly altered CovR occupancy between wild-type and deltaSpxA2 (FDR < 0.05), with class-specific enrichment of CovR dimer and monomer binding motifs consistent with the two-class CovR binding model (Horstmann et al. 2023). These data contribute to a multi-omic analysis including RNA-seq, DIA proteomics, and NanoString nCounter that defines the regulatory roles of SpxA1 and SpxA2 in GAS 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