Landeta Lab
Principal Investigator: Cristina Landeta
Institution: Indiana University (Bloomington, IN)
Primary Subfield: Molecular & Cell Bio
Recruitment Status: ✅ Hiring Postdocs
Research Focus
Oxidative protein folding in bacteria PROJECT SUMMARY Oxidative protein folding generates covalent linkages between the sulfur atoms of two cysteine residues, known as disulfide bonds (DSBs). DSBs play a crucial role in the three-dimensional structure and biological function of exported proteins in prokaryotes and eukaryotes. Since the discovery of the first DSB catalyst in the bacterium Escherichia coli, bacteria have been proven to be a powerful model system for understanding the molecular mechanisms that drive DSB formation. Our research aims to address three key questions in the field: 1) What principles enable productive thiol oxidation in essential proteins when canonical DSB-forming enzymes are inactive? 2) What proteins depend on DSBs in complex cell envelopes? and 3) Do distinct thiol-disulfide oxidoreductases exhibit substrate specificity? My lab employs a multidisciplinary approach to dissect the fundamental mechanisms and consequences of DSB formation in vivo using bacteria. As model systems for our basic research program, we employ two model organisms, the Gram-negative bacterium E. coli and the acid-fast bacterium Mycobacterium smegmatis, because (1) they each express…
Active NIH Awards
- 1R35GM161411-01: Oxidative protein folding in bacteria (2026)
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