Emanuel Goldman graduated with honors from the Bronx High School of Science in 1962,
received a B.A. cum laude from Brandeis University in 1966, where he was a chemistry
major, and he completed his Ph.D. in Biochemistry at M.I.T. in 1972. He did postdoctoral
research at Harvard Medical School and at the University of California, Irvine, before
joining the faculty of New Jersey Medical School in 1979, where he rose through the ranks
to Professor in 1993. Among his awards and honors, he was a Damon Runyon Fellow, A Lievre
Senior Fellow of the California Division- American Cancer Society, and a recipient of a
Research Career Development Award from the National Cancer Institute. Among his service
activities, he was an officer and organizer of the NY-NJ Molecular Biology Club, served as a full
member of an American Cancer Society Study Section, and continues to serve on the editorial boards
of "Protein Expression and Purification", and "Applied and Environmental Microbiology". He was also
twice elected by his colleagues to serve as President of the university chapter of American
Association of University Professors, and he was elected to serve as Vice President and
subsequently President of the Faculty Organization of NJMS. He published a Comment in Lancet July
2020 (https://www.thelancet.com/journals/laninf/article/PIIS1473-3099(20)30561-2/fulltext) that began
the process of reversing the mistaken belief that COVID-19 was transmitted from surfaces.
Ph.D., 1972, Massachusetts Institute of Technology B.A., 1966, Brandeis University
SARS-CoV2/COVID-19 related articles: Lancet Comment (2020):
Applied and Environmental Microbiology Commentary (2021):
AEM Research paper using Phi6 as surrogate (2021):
Goldman E (September 2011) tRNA and the Human Genome [revised]. In: Encyclopedia of Life
Sciences, John Wiley & Sons, Ltd: Chichester UK (6 pages) http://www.els.net/ [DOI:
Goldman E (September 2008) Transfer RNA [revised]. In: Encyclopedia of Life Sciences, John Wiley
& Sons, Ltd: Chichester UK (11 pages) http://www.els.net/
Goldman E (December 2008) Translation Control by RNA [revised]. In: Encyclopedia of Life Sciences,
John Wiley & Sons, Ltd: Chichester UK (13 pages), http://www.els.net/ [DOI:
Goldman E (December 2007) Translation Control by Proteins [revised]. In: Encyclopedia of Life
Sciences, John Wiley & Sons, Ltd: Chichester UK (9 pages) http://www.els.net/
Rojiani, M., Jakubowski, H. and Goldman, E. (1990) Relationship between protein synthesis and con?
centrations of charged and uncharged tRNATrp in E. coli. Proceedings of the National Academy of
Sciences of the USA 87:1511 1515.
Goldman, E. and Jakubowski H. (1990) Uncharged tRNA , protein synthesis, and the bacterial
stringent response. Molecular Microbiology 4:2035-2040
Shu P, Dai H, Gao W, Goldman E. (2006) Inhibition of translation by consecutive rare leucine codons
in E. coli: Absence of effect of varying mRNA stability. Gene Expression 13: 97-106.
Shu P, Dai H, Mandecki W, Goldman E. (2004) CCC CGA is a Weak Translational Recoding Site in
Escherichia coli. Gene 343:127-132.
Song L, Mandecki, W, Goldman, E. (2003) Expression of non-open reading frames isolated from
phage display due to translation reinitiation. FASEB Journal 17: 1674-1681.
Goldman, E., Korus, M. and Mandecki, W. (2000) Efficiencies of translation in three reading frames of
unusual non ORF sequences isolated from phage display. FASEB Journal 14:603-611.
Gao, W. and Goldman, E. (1997) Use of SDS-polyacrylamide gel electrophoresis to resolve mRNA
and its protein product in one gel. FASEB Journal 11:1153-1156.
Gao, W., Tyagi, S., Kramer, F.R. and Goldman, E. (1997) Messenger RNA release from ribosomes
during 5'-translational blockage by consecutive low-usage arginine but not leucine codons in
Escherichia coli. Molecular Microbiology 25:707-716. Erratum: (1998) 27:669.
Gao, W., Jakubowski, H. and Goldman, E. (1995) Evidence that uncharged tRNA can inhibit a
programmed translational frameshift in Escherichia coli. Journal of Molecular Biology 251:210-216.
Goldman, E., Rosenberg, A., Zubay, G. and Studier, F.W. (1995) Consecutive low-usage leucine
codons block translation only when near the 5' end of a message in E. coli. Journal of Molecular
Sipley, J. and Goldman, E. (1993) Increased ribosomal accuracy increases a programmed
translational frameshift in Escherichia coli. Proceedings of the National Academy of Sciences of the
Sipley, J., Dunn, J. and Goldman, E. (1991) Bacteriophage T7 morphogenesis and gene 10 frame-
shifting in E. coli with different ribosomal fidelity conditions. Molecular and General Genetics 230:376-
Rojiani, M., Jakubowski, H. and Goldman, E. (1989) Effect of variation of charged and uncharged
tRNATrp levels on ppGpp synthesis in Escherichia coli. Journal of Bacteriology 171:6493-6502.
Jakubowski, H. and Goldman, E. (1984) Quantities of individual aminoacyl tRNA families and their
turnover in Escherichia coli. Journal of Bacteriology 158:769-776.
Areas Of Interest
A FRET assay for antibiotic drug leads binding EF-Tu and tRNA of E. coli
Many bacterial diseases have become more deadly as the bacteria have developed resistance to treatment with antibiotics. The proposed research is likely to lead to the identification of an entirely new class of antibiotics that will provide the public with new protection from these dangerous diseases and will directly impact therapies.
Along with collaborator Wlodek Mandecki (Co-Principal Investigator), the method proposed in the current project allows for an identification of drug leads for the treatment of bacterial infection. The identified compound(s) will inhibit the function of the microbe's protein synthesis machinery by blocking the activity of a required ternary complex that includes the molecules EF-Tu and tRNA, as well as GTP. As such, the compound(s) will inhibit protein biosynthesis in the infectious microorganism. About half of all antibiotics target bacterial protein synthesis, but there are no inhibitors currently in use in clinical practice that target this particular step.
By modifying EF-Tu genetically, and with attachment of fluorescent dyes to the modified EF-Tu and one of the cell's tRNAs, tRNAPhe, we have been able to demonstrate "fluorescence resonance energy transfer" (FRET) upon formation of the ternary complex. Further, the modified molecules appear to be capable of carrying out their function in protein synthesis normally. These reagents are thus a powerful tool for rapid high-throughput screening (HTS) of libraries of small molecules capable of inhibiting ternary complex formation because any inhibitor will prevent FRET from being observed.
Because ternary complex formation between EF-Tu, tRNA, and GTP is a universal requisite for protein synthesis, there is reason to expect that antibiotics identified in this project will have broad specificity. Although human cells also require ternary complex formation, the human versions of these molecules are sufficiently different from bacterial forms that we expect to find chemicals that affect bacteria but not humans. Indeed, there are many inhibitors of bacterial protein synthesis that do not inhibit human protein synthesis.
EF-Tu is an ideal target for the development of novel antibacterial agents because the protein is essential and highly conserved among bacteria. Among the pathogens that could be treated by the drug leads identified in this project are E. coli O157:H7, and Klebsiella pneumoniae, among others. Increased antibiotic resistance has threatened our ability to treat diseases caused by these bacteria. This has become a critical concern with the recent emergence of resistance to antibiotics of last resort, carbapenems. "Superbugs" carrying this resistance are also resistant to almost all known antibiotics in clinical use and are a significant threat to public health. Thus, there is urgent need for the development of new antibiotics such as the drug leads we propose to identify.
See also: Chudaev M, Poruri K, Goldman E, Jakubowski H, Jain MR, Chen W, Li H, Tyagi S, Mandecki W. (2013) Design and properties of efficient tRNA:EF-Tu FRET system for studies of ribosomal translation. Protein Engineering, Design and Selection 26:347-57.