All Publications
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The Prion-Like Properties of the INO80 Chromatin Remodeler Regulate Metabolic Gene Expression.
bioRxiv : the preprint server for biology
2026
Abstract
The INO80 chromatin-remodeling complex is a multi-subunit regulator of DNA-templated processes, yet the mechanisms that control remodeler function in vivo are not completely known. In this study, we report that the Ies6 subunit of the INO80 complex encodes a prion-like domain (PLD) within a larger region of predicted disorder. After transient inducible overexpression, both full-length Ies6 and the PLD domain alone aggregate in a manner that evades proteasome-mediated degradation, suggestive of prion-like behavior. Cytosolic aggregates are also visible with fluorescent microscopy following expression of the PLD alone. Loss of the protein chaperone Hsp70 increases Ies6 aggregation. In addition, deletion of ARP5, another INO80 subunit and binding partner of Ies6, also results in elevated protein aggregation. Finally, transcriptome analysis indicates that loss of PLD-mediated aggregation alters the expression of metabolic stress-responsive genes, including glucose-starvation and respiratory programs, even in glucose-replete conditions. Together, these findings support a model in which Ies6 couples the INO80 complex to metabolic gene regulation via prion-like behavior, providing a potential new mechanism for tuning chromatin-based metabolic adaptation.
View details for DOI 10.64898/2026.05.18.722789
View details for PubMedID 42239227
View details for PubMedCentralID PMC13228451
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Acetyl-CoA Synthetase 1 regulates global histone propionylation and metabolic stress responses.
bioRxiv : the preprint server for biology
2026
Abstract
Cells and organisms are often exposed to various metabolic environments that require adaptive responses for survival. One common way cells adapt to fluctuating nutrient environments is through regulated transcription of metabolic genes. Intermediary metabolites, such as acetyl-CoA, produced by metabolic pathways, serve as cofactors for histone post-translational modifications, which in turn regulate gene expression. However, increasing evidence shows that non-acetyl acyl-CoAs, such as propionyl-CoA, participate in gene regulation during metabolic stress. In this report, we find that histone propionylation functions as a global response to glucose starvation. Furthermore, we find that Acetyl-CoA Synthetase 1 (Acs1) binds chromatin and is the primary enzyme responsible for generating propionyl-CoA in the nucleus. Together, our findings reveal that Acs1-mediated histone propionylation constitutes a novel pathway for metabolic adaptation, linking nutrient availability to chromatin modification.
View details for DOI 10.64898/2026.05.05.722790
View details for PubMedID 42146428
View details for PubMedCentralID PMC13174532
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Revolutionizing Postdoctoral Training Using the Social Ecological Model: Insights and Experiences from the Propel Scholars.
GEN biotechnology
2024; 3 (4): 196-206
Abstract
The dissatisfaction within the postdoctoral training phase has led to the drastic reduction in the number of U.S. citizens pursuing postdoctoral positions within the biological and biomedical sciences fields. Even more so, there is an obvious disparity in not only the recruitment but the retention among underrepresented groups to pursue careers as academic scientists. The proposed social-ecological model and National Institute of Health advisory committee suggests reforming the postdoctoral training phase to overcome these downward trends and disparities. Importantly, some programs like the Stanford Propel Postdoctoral Program were integrating this framework and recommendations without knowledge that they would be released 2 years later. The goal of the Propel Program is to provide social, cohort, financial, and institutional support to diverse cohorts of postdoctoral trainee to diversify the professoriate. Within this piece, several of the Propel scholars come together to provide their perspectives on how the Propel Program has benefited their postdoctoral training experience.
View details for DOI 10.1089/genbio.2024.0014
View details for PubMedID 40709103
View details for PubMedCentralID PMC12288851