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Emily Weinert

Professor of Biochemistry and Molecular Biology, and of Chemistry
Emily Weinert

About Me

Emily Weinert graduated from Duke University in 2002 with a B.Sc. in Chemistry after working with Professor John Simon. She then joined Professor Steve Rokita’s group at the University of Maryland for her Ph.D. At the end of 2006, Emily began her postdoctoral work in Professor Michael Marletta’s laboratory at the University of California, Berkeley. She joined the faculty of Emory University in 2011 where she worked for 8 years prior to moving to Penn State University.



Department or University Committees

  • Graduate Steering Committee

  • Graduate Recruiting Committee



Program or Departmental Affiliations

The BMMB Graduate Program The Molecular, Cellular, and Integrative Program The Chemistry Department




Huck Institutes of Life Sciences Microbiome Center



Research Summary

Bacterial Oxygen Sensing

The ability of heme proteins to reversibly bind diatomic ligands allows organisms to sense changes in their environment. Recently, changes in gaseous ligand concentrations have been proposed to be involved in the pathogenesis of a variety of bacteria. Our work focuses on understanding how the globin coupled sensor protein family senses oxygen and transmits the binding signal into downstream events. Understanding how these diatomic signals are transduced will elucidate the role of heme sensors in bacterial signaling pathways and pathogenesis, as well as potentially yield starting points for the development of novel antibacterial agents. 

Atypical Cyclic Nucleotides

Nucleotides play a number of important roles as second messengers involved in both eukaryotic and prokaryotic signaling. Mounting evidence suggests that there may be additional nucleotide signaling pathways but very little is known about the proteins involved. Our work aims to identify new cyclic nucleotide-dependent pathways in bacteria, including the proteins and signals involved in sensing cNMPs and regulating cNMP levels. These studies provide basic insights into novel cellular signaling pathways and metabolism, as well as the phenotypes controlled by cNMPs. 



Honors and Awards

  • Emory Crystal Apple Award for Excellence in Graduate Education (2017)
  • National Science Foundation CAREER Award (8/2014 - 7/2019)
  • Ruth L. Kirschstein National Research Service Award Individual Fellowship (09/2007 -9/2010)



Selected Publications

  • Fontaine, B.M.; Duggal, Y.; Weinert, E.E. (2018) Exploring the Links between Nucleotide Signaling and Quorum Sensing Pathways in Regulating Bacterial Virulence. ACS Infect. Dis. 4, 1645-1655. DOI: 10.1021/acsinfecdis.8b00255
  • Rivera, S.; Paul, P.G.; Hoffer, E.D.; Vansuch, G.E.; Metzler, C.L.; Dunham, C.M.; Weinert, E.E. (2018) Structural Insights into Oxygen-Dependent Signal Transduction within Globin Coupled Sensors. Inorg. Chem. 57, 14386-14395. DOI: 10.1021/acs.inorgchem.8b02584
  • Fontaine, B.M.; Martin, K.S.; Garcia-Rodriguez, J.M.; Jung, C.; Briggs, L.; Southwell, J.E.; Jia, X.; Weinert, E.E. (2018) RNase I Regulates E. coli 2′,3′-Cyclic Nucleotide Monophosphate Levels and Biofilm Formation. Biochem. J. 475, 1491-1506. DOI: 10.1042/BCJ20170906
  • Walker, J.A.; Rivera, S.; Weinert, E.E. (2017) Mechanism and Role of Globin Coupled Sensor Signaling. Adv. Microb. Physiol. 71, 133-169. DOI: 10.1016/bs.ampbs.2017.05.003
  • Burns, J.L.; Jariwala, P.B.; Rivera, S.; Fontaine, B.M.; Briggs, L.; Weinert, E.E. (2017) Oxygen-Dependent Globin Coupled Sensor Signaling Modulates Motility and Virulence of the Plant Pathogen Pectobacterium carotovorumACS Chem. Biol. 12, 2070-2077. DOI: 10.1021/acschembio.7b00380
  • Jia, X.; Wang, J.-b.; Rivera, S.; Duong, D.; Weinert, E.E. (2016) An O2-sensing stressosome from a Gram-negative bacterium. Nature Commun. 7, 12381. DOI: 10.1038/ncomms12381
  • Burns, J.L.; Rivera, S.; Deer, D.D.; Joynt, S.C.; Dvorak, D.; Weinert, E.E. (2016) Oxygen and c-di-GMP Binding Control Oligomerization State Equilibria of Diguanylate Cyclase-Containing Globin Coupled Sensors. Biochemistry. 55, 6642-6651. DOI: 10.1021/acs.biochem.6b00526