Amy Gehring

Photo of Amy Gehring

Philip and Dorothy Schein Professor of Chemistry, Director of the Science Center

Hopper Science Center Rm 115
At Williams since 2002

Lab: Hopper Science Center 113
(413) 597-2184


B.A. Williams College (1994)
Ph.D. Harvard University, Bio Chem & Molecular Pharmacol (1998)
Postdoctoral Fellow at Harvard University (2002)

Areas of Expertise

If you have smelled fresh dirt, you have already been introduced to bacteria of the genus Streptomyces. In addition to producing the characteristic odor of dirt, these common soil bacteria manufacture the majority of known antibiotics. These medicinally-important compounds are produced during the course of the bacteriumÅfs unusual and complicated life cycle that culminates in sporulation. Research in my lab involves understanding the regulation of this developmental process and concurrent antibiotic production in the model organism Streptomyces coelicolor. Beginning with mutant strains that are defective in certain aspects of development, we have identified genes and thereby proteins that are necessary to progress through the various stages of the bacteriumÅfs life cycle. Current projects in the lab include (1) using proteomics approaches including 2D gel electrophoresis and MALDI-TOF mass spectrometry to characterize changes in the cell resulting from activity of a stress response sigma factor; (2) characterizing the activity of a potential transcription factor required for sporulation; and (3) assaying the effects of various mutations on antibiotic production.

Scholarship/Creative Work

Selected Publications

  • Lu, Y., San Roman, A.K., and Gehring, A.M. (2008) Role of phosphopantetheinyl transferase genes in antibiotic production by Streptomyces coelicolor. J. Bacteriol. 190, 6903-6908.
  • Gordon, N.D., Ottaviano, G.L., Connell, S.E., Tobkin, G.V., Son, C.H., Shterental, S. and Gehring, A.M. (2008) Secreted-protein response to σU activity in Streptomyces coelicolor. J. Bacteriol. 190, 894-904.
  • Dominy, J.E., Jr., Simmons , C.R., Karplus, P.A., Gehring, A.M., and Stipanuk, M.H. (2006) Identification and characterization of bacterial cysteine dioxygenases (CDOs): a new route of cysteine degradation for eubacteria. J. Bacteriol. 188, 5561-5569.
  • Gehring, A.M., Wang, S.T., Kearns, D.B., Storer, N.Y., and Losick, R. (2004) Novel Genes that Influence Development in Streptomyces Coelicolor. J. Bacteriol. 186, 3570-3577.
  • Gehring, A.M., Yoo, N.J., and Losick, R. (2001) RNA polymerase sigma factor that blocks morphological differentiation by Streptomyces coelicolor. J. Bacteriol. 183, 5991-5996.
  • Gehring, A.M., Nodwell, J.R., Beverley, S.M., and Losick, R. (2000) Genomewide insertional mutagenesis in Streptomyces coelicolor reveals additional genes involved in morphological differentiation. Proc. Natl. Acad. Sci. USA 97, 9642-9647.
  • Shaw-Reid, C.A., Kelleher, N.L., Losey, H.C., Gehring, A.M., Berg, C., and Walsh, C.T. (1999) Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization. Chemistry & Biology 6, 385-400.
  • Ehmann, D.E., Gehring, A.M., and Walsh, C.T. (1999) Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of a-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38, 6171-6177.
  • Sinha Roy, R., Gehring, A.M., Milne, J.C., Belshaw, P.J., and Walsh, C.T. (1999) Thiazole and oxazole peptides: biosynthesis and molecular machinery. Nat. Prod. Rep. 16, 249-263.
  • Huang, L., Kumura Ishii, K., Zuccola, H., Gehring, A.M., Hwang, C.B.C., Hogle, J., and Coen, D.M. (1999) The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: relationship to the structure of a-like polymerases. Proc. Natl. Acad. Sci. USA 96, 447-452.
  • Gehring, A.M., DeMoll, E., Fetherston, J.D., Mori, I., Mayhew, G.F., Blattner, F.R., Walsh, C.T., and Perry, R.D. (1998) Iron acquisition in plague: modular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis. Chemistry & Biology 5, 573-586.
  • Gehring, A.M., Mori, I., Perry, R.D., and Walsh, C.T. (1998) The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 37, 11637-11650. (Journal correction: (1998) 37, 17104.)
  • Ritsema, T., Gehring, A.M., Stuitje, A.R., van der Drift, K.M.G.M., Dandal, I., Lambalot, R.H., Walsh, C.T., Thomas-Oates, J.E., Lugtenberg, B.J.J., and Spaink, H.P. (1998) Functional analysis of an interspecies chimera of acyl carrier proteins indicates a specialized domain for protein recognition. Mol. Gen. Genet. 257, 641-648.
  • Gehring, A.M., Mori, I., and Walsh, C.T. (1998) Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 37, 2648-2659.
  • Carreras, C.W., Gehring, A.M., Walsh, C.T., and Khosla, C. (1997) Utilization of enzymatically phosphopantetheinylated acyl carrier proteins and acetyl-acyl carrier proteins by the actinorhodin polyketide synthase. Biochemistry 36, 11757-11761.
  • Walsh, C.T., Gehring, A.M., Weinreb, P.H., Quadri, L.E.N., and Flugel, R.S. (1997) Post-translational modification of polyketide and nonribosomal peptide synthases. Curr. Op. Chem. Biol. 1, 309-315.
  • Gehring, A.M., Bradley, K.A., and Walsh, C.T. (1997) Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 36, 8495-8503.
  • Gehring, A.M., Lambalot, R.H., Vogel, K.W., Drueckhammer, D.G., and Walsh, C.T. (1997) Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase. Chemistry & Biology 4, 17-24.
  • Carter, C.A., Forney, R.W., Gray, E.A., Gehring, A.M., Schneider, T.L., Young, D.B., Lovett, C.M., Jr., Scott, L., Messer, A.C., and Richardson, D.P. (1997) Toxicarioside A. A new cardenolide isolated from Antiaris toxicaria latex-derived dart poison. Assignment of the 1H-and 13C-NMR shifts for an antiarigenin aglycone. Tetrahedron 53, 13557-13566.

Previous Courses Taught

  • 115: AIDS: The Disease and Search for a Cure
  • 153: Concepts of Chemistry: Advanced Section
  • 321: Biochemistry I: Structure and Function of Biological Molecules
  • 324: Enzyme Kinetics and Reaction Mechanisms
  • BIMO 401: Topics in Biochemistry and Molecular Biology