Division of ScienceDepartment
Marshak Science Building MR616 (office) | MR620 (lab)
p: 212-650-8553 (office)
p: 212-650-8554 (lab)
Dr. Janakiraman uses Escherichia coli as a model system to examine bacterial cell division. Her lab is characterizing key proteins that are required for the spatio-temporal localization of the FtsZ ring structure at midcell. The FtsZ ring serves as a framework for assembly of the rest of the division machinery. Her laboratory is investigating the regulatory events that result in optimal FtsZ ring dynamics in vivo, by studying the molecular interactions amongst FtsZ ring stabilizers and inhibitors.
Postdoctoral, Mass. General Hospital / Harvard Medical School, 2006
Ph.D. in Microbiology, University of Illinois at Urbana-Champaign, 2001
Biology 35000 - Microbiology
Biology C0300 - Molecular Biology (Graduate Level)
In Escherichia coli, cell division requires the assembly of a large number of proteins at midcell. These proteins are involved in chromosome segregation, septum formation, and binary cell division. The earliest identified event in bacterial cytokinesis is the polymerization of a ring structure (FtsZ ring) at midcell by FtsZ, a tubulin-like GTPase. The FtsZ ring serves as a framework for assembly of the rest of the division machinery. The assembly dynamics of FtsZ are influenced by a large group of FtsZ-regulatory proteins that ensure the spatial and temporal integrity of the FtsZ ring. Our laboratory is investigating the regulatory events that result in optimal FtsZ ring dynamics in vivo, by studying the molecular interactions amongst FtsZ ring stabilizers and inhibitors. Using molecular biology, genetics, microscopy and biochemical techniques, we are examining not only how FtsZ assembly dynamics are maintained in E. coli but also the general molecular mechanisms that regulate spatial localization of bacterial proteins.
Fixen, K.R., A. Janakiraman, S.J. Garrity, D. J. Slade, A. N. Gray, N. Karahan, A. Hochschild, and M.B. Goldberg. 2011. Extracytoplasmic signaling by a cell division protein in the establishment of bacterial polarity. (Submitted)
Duand-Heredia J., H. H. Yu, S. De Carlo, C. F. Lesser, and A. Janakiraman. 2011. Identification of ZapC, a stabilizer of the FtsZ-ring in Escherichia coli. J. Bacteriol., 193 (6):1405-1413.
Janakiraman, A., K.R. Fixen, A.N. Gray, H. Niki and M.B. Goldberg. 2009. Genome-scale proteomic screen identifies role for DnaK in chaperoning of polar autotransporters in Shigella. J. Bacteriol., 191 (20):6300-6311.
Nie, L., Y. Ren, A. Janakiraman, S. Smith, and H. Schulz. 2008. A Novel Paradigm of Fatty Acid ß-Oxidation Exemplified by the Thioesterase-catalyzed Partial Degradation of Conjugated Linoleic Acid That Fully Supports Growth of E. coli. Biochemistry. 47(36):9618-9626.
Janakiraman, A., J. Ikeda, D.G. Kehres, M.E. Maguire and J. M. Slauch. 2005. Transcriptional regulation of sitABCD of Salmonella enterica serovar Typhimurium by MntR and Fur. J. Bacteriol., 187 (3):912-922.
Janakiraman, A. and M. B. Goldberg. 2004. Recent advances on the development of bacterial poles. Trends Microbiol., 12 (11):518-525.
Janakiraman, A. and M.B. Goldberg. 2004. Evidence for polar positional information in E. coli independent of cell division and nucleoid occlusion. Proc. Natl. Acad. Sci., 101(3):835-840.
Research Scientist: Eugene Rivkin
Research Associate: Jorge Durand-Heredia
Graduate Student: Guoxiang Fan
Undergraduates: Helen Yu, Cheryl Mazzeo