PhD Institution: The University of Iowa, Chemistry Department
I am interested in understanding the mechanisms involved in bacterial cell division, especially how biochemical (catalytic) events cause morphological changes. My research focuses on SPOR proteins, which specifically interact with septal peptidoglycan (PG) and other cell division proteins. Deleting SPOR proteins causes morphological and cell division defects and their timely localization at septum via interacting with PG is important for efficient and correct cell division. I am currently applying my chemistry and biochemistry knowledge to elucidate the molecular function of SPOR proteins.
Yahashiri, A., Jorgenson, M.A., and Weiss, D.S. Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides, Proc. Natl. Acad. Sci. USA, 2015 in press.
Jorgenson, M.A., Chen, Y., Yahashiri, A., Popham, D.L., and Weiss, D.S. The Bacterial Septal Ring Protein RlpA is a Lytic Transglycosylase that Contributes to Rod Shape and Daughter Cell Separation in Pseudomonas aeruginosa, Mol. Microbiol., 2014, 93(1), 113-128.
Yahashiri, A., Rubach, J.K., and Plapp, B.V., Effects of cavities at the nicotinamide binding site of liver alcohol dehydrogenase on structure, dynamics and catalysis. Biochemistry, 2014, 53(5), 881-94.
Duncan, T.R.*, Yahashiri, A.*, Arends, R.S.J., Popham, D.L., and Weiss, D.S., The Cell Division Protein FtsN: Identification of SPOR Domain Amino Acids Important for Septal Localization, Peptidoglycan-binding, and a Disulfide Bond, J. Bacteriol. 2013, 195(23), 5308-15. *These Authors Contributed Equally
Williams, K.B.*, Yahashiri, A.*, Arends, R.S.J., Popham, D.L., Fowler, A.C., and Weiss, D.S., Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: Insights into Septal Localization, Biochemistry, 2013, 52, 627–639. *These Authors Contributed Equally
Sen, A.*, Yahasiri, A.*, and Kohen, A., Triple isotopic labeling and kinetic isotope effects: a sensitive and accurate method for exposing H-transfer steps in enzymatic systems, Biochemistry, 2011, 50, 6462–6468. *These Authors Contributed Equally
Yahashiri, A., Nimrod, G., Ben-Tal, N., Howell, E.E., and Kohen, A., Effect of electrostatic shielding on H-tunneling in R67 dihydrofolate, ChemBioChem, 2009, 10, 2620-2623.
Yahashiri, A., Sen, A., and Kohen, A., Microscale synthesis and kinetic isotope effect analysis of (4R)-[Ad-14C, 4-2H] NADPH and (4R)-[Ad-3H,4-2H] NADPH, J. Labeled Comp. Radiopharma, 2009, 52, 463-466.
Yahashiri, A., Howell, E.E., and Kohen, A., Tuning of the H-Transfer Coordinate in Primitive versus Well-Evolved Enzymes, ChemPhysChem, 2008, 9, 980-982.