Faith H. Lessner
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Also affiliated: University of Iowa (2006); Pennsylvania State University (2006–2007); University of British Columbia (2006); University of Washington (2006)
Research Areas
Biomedical Subjects
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Biography and Research Information
OverviewAI-generated summary
Faith H. Lessner's research investigates fundamental biological processes in microorganisms, focusing on gene expression regulation, protein function, and metabolic pathways. Her work has explored the mechanisms controlling photosynthesis gene expression in purple alphaproteobacteria, such as *Rhodopseudomonas palustris*, identifying repressors like PpsR that govern these processes. Lessner has also studied the biogenesis and function of iron-sulfur clusters, essential components in many proteins, particularly within anaerobic archaea like *Methanosarcina acetivorans*. Her investigations include the characterization of the ISC system for iron-sulfur cluster assembly and the identification of thioredoxin systems involved in cellular redox balance in these organisms. Additionally, her research has examined the expression and tolerance of bacterial enzymes, such as catalase, in anaerobic methanogens when exposed to reactive oxygen species. Lessner's scholarship metrics include an h-index of 8, with 9 total publications and 196 total citations.
Metrics
- h-index: 8
- Publications: 9
- Citations: 196
Selected Publications
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The Razorback Educator (2026)Journal of the Arkansas Academy of Science OpenAlex
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Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis (2020)
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Genes essential for phototrophic growth by a purple alphaproteobacterium (2017)
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Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions (2016)
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The [4Fe‐4S] clusters of Rpo3 are key determinants in the post Rpo3/Rpo11 heterodimer formation of RNA polymerase in <i>Methanosarcina acetivorans</i> (2016)
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Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen (2013)
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Subunit D of RNA Polymerase from Methanosarcina acetivorans Contains Two Oxygen-labile [4Fe-4S] Clusters (2012)
Collaboration Network
Top Collaborators
- Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen
- Subunit D of RNA Polymerase from Methanosarcina acetivorans Contains Two Oxygen-labile [4Fe-4S] Clusters
- Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis
- Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions
- The [4Fe‐4S] clusters of Rpo3 are key determinants in the post Rpo3/Rpo11 heterodimer formation of RNA polymerase in <i>Methanosarcina acetivorans</i>
- Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen
- Subunit D of RNA Polymerase from Methanosarcina acetivorans Contains Two Oxygen-labile [4Fe-4S] Clusters
- The [4Fe‐4S] clusters of Rpo3 are key determinants in the post Rpo3/Rpo11 heterodimer formation of RNA polymerase in <i>Methanosarcina acetivorans</i>
- The Razorback Educator
- The Razorback Educator
- Subunit D of RNA Polymerase from Methanosarcina acetivorans Contains Two Oxygen-labile [4Fe-4S] Clusters
- Subunit D of RNA Polymerase from Methanosarcina acetivorans Contains Two Oxygen-labile [4Fe-4S] Clusters
- Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen
- Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen
- The [4Fe‐4S] clusters of Rpo3 are key determinants in the post Rpo3/Rpo11 heterodimer formation of RNA polymerase in <i>Methanosarcina acetivorans</i>
- Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions
- Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions
- Genes essential for phototrophic growth by a purple alphaproteobacterium
- Genes essential for phototrophic growth by a purple alphaproteobacterium
- Genes essential for phototrophic growth by a purple alphaproteobacterium
- Genes essential for phototrophic growth by a purple alphaproteobacterium
- Genes essential for phototrophic growth by a purple alphaproteobacterium
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