Jodi L. Camberg


Molecular Mechanisms of Energy-Dependent Proteins during Essential Cell Processes
Energy-dependent molecular machines are proteins that harness chemical energy released upon nucleotide hydrolysis and translate that energy into mechanical work. Molecular machines are involved in every cellular process, such as genetic replication, establishment and maintenance of the proteome, molecular transport, motility, respiration, growth and division. My research is focused on determining how energy-dependent molecular machines accomplish vital tasks, how these tasks influence the compendium of cellular processes, and the interplay between these cellular processes and the components involved.

Cell Division in Bacteria
The cell division pathway is an example of a complex cellular process that requires the contributing activities of many molecular machines. These activities must be precisely coordinated and regulated both spatially and temporally for cells to divide. In bacteria, the process of division, or cytokinesis, entails multiple steps, including assembly of division protein complexes at midcell, membrane constriction, insertion of new cell wall components and separation of daughter cells. Our laboratory is interested in studying the biochemical mechanisms of proteins that modulate the cellular position of the division machinery, referred to as the Min system, as well as the machinery that promotes constriction (FtsZ and FtsZ-interacting proteins).

Regulated Proteolysis
Protein degradation is utilized by the cell to maintain the cellular proteome and promote homeostasis. Regulated proteolysis can be used to control cellular responses to stimuli and modulate cellular processes. The ATP-dependent chaperone protease complex known as ClpXP is a molecular machine that unfolds protein substrates bearing specific recognition tags and degrades them. One substrate degraded by ClpXP in E. coli is the essential protein FtsZ. Our lab is working on how degradation of cell division proteins such as FtsZ modulates the process of cell division in E. coli. This work will not only lead to a better understanding of the fundamental process of cell division, but will also lead to a better understanding of the biochemical mechanisms of substrate recognition and protein unfolding by ATP-dependent molecular chaperones and degradation by cognate proteases.


  • Research Fellow in Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, 2005-2012
  • Research Fellow with University of Maryland School of Medicine at the Jerome H. Holland Laboratory of the American Red Cross, Rockville, MD, 2004-2005
  • Ph.D., Biochemistry, The George Washington University, 2004
  • B.Sc., Biochemistry and Molecular Biology, The Pennsylvania State University, 2000

Selected Publications

LaBreck CJ, May S, Viola M, Conti J, Camberg JL. The ATP-dependent chaperone ClpX targets native and non-native aggregated substrates for remodeling, disassembly, reactivation and degradation. Frontiers in Molecular Biosciences. 2017 May 4;4:26.

Viola MG, LaBreck CJ, Conti J, Camberg JL. Proteolysis-dependent remodeling of the tubulin homolog FtsZ at the division septum in Escherichia coli. PLOS One. 2017 Jan 23; 12(1):e0170505.

Rule CS, Patrick M, Camberg JL, Maricic N, Hol WH, Sandkvist M. Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE. MicrobiologyOpen. 2016; 10.1002/mbo3.376.

Leatham-Jensen MP, Mokszycki ME, Rowley DC, Deering R, Camberg JL, Sokurenko EV, Tchesnokova VL, Fridmodt-Møller J, Krogfelt KA, Nielsen KL, Fridmont-Møller N, Sun G, Cohen PS. Uropathogenic Escherichia coli metabolite-dependent quiescence and persistence may explain antibiotic tolerance during urinary tract infection. mSphere. 2016; 1(1):e00055-15.

Conti J, Viola MG, Camberg JL. The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. FEBS Letters. 2015; 589(2): 201-206.

Camberg JL, Viola MG, Rea L, Hoskins JR, Wickner S. Location of dual sites in FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker. PLOS One. 2014; 9(4): e94964.

Genest O, Reidy M, Street TO, Hoskins JR, Camberg JL, Agard D, Masison D, Wickner S. Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. Molecular Cell. 2013; 49(3): 464-473.

Camberg JL, Wickner S. Regulated proteolysis as a force to control the cell cycle. Structure. 2012; 20(7): 1128-30.

Genest OP, Hoskins JR, Camberg JL, Doyle SM, Wickner S. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in protein remodeling. Proc. Natl. Acad. Sci. USA. 2011; 108(20): 8206-11.

Camberg JL, Hoskins JR, Wickner S. The interplay of ClpXP with the cell division machinery in Escherichia coli. J Bacteriol. 2011; 193(8): 1911-18. Highlighted in Microbe magazine (ASM Press), May 2011: “Backup Systems Keep Bacteria Dividing and Multiplying when Critical Parts Malfunction”

Camberg JL, Hoskins JR, Wickner S. ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. USA. 2009; 106(26): 10614-9.

Camberg JL, Johnson TL, Patrick M, Abendroth J, Hol WGJ, Sandkvist M. Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids. EMBO J. 2007; 26(1): 19-27.

Camberg JL, Sandkvist M. Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE. J Bacteriol. 2005 Jan; 187(1): 249-56.