My group uses the model organism E. coli to study basic cellular physiology with a focus on ribosome function. In all cells, these machines decode genetic material and make proteins in a process called translation. Because ribosomes are the target of many antibiotics, there has been extensive research into the mechanism ribosome function to understand how these drugs work and how microbes become resistant to them. However, there are several other highly conserved features of ribosomes (and factors associated with their assembly) that are important for protein synthesis, but the details of their activities have not been established and no drugs are known that influence their activities.

Our goal is to establish the molecular mechanisms for several of these translation-related factors, including some proteins that are part of the ribosome and some that are implicated in helping the ribosomes get built. This information is important because it will allow researchers to explore new antibiotic targets and also to have a comprehensive model of protein synthesis in the study of disease.

A typical strategy we employ is to use genetic systems to reveal the physiological pathways affected by translation factors, and then to interrogate those pathways using a combination of molecular biology, computational biology, and biochemistry. The lab has hosted several graduate students and many undergraduates for this research effort.

In addition studies of protein synthesis, we also have an Applied Industrial Microbiology (AIM) program. AIM uses a collection of student-driven projects to combine classical microbiology with advanced molecular biology to put students in touch with industry before they graduate. Some examples include: identifying microbes responsible for food production and for detoxifying wastewater in bioreactors, identifying fungi that produce new medically important molecules, and studying the effects of microgravity on microbial physiology.

Recent Publications

  1. S.D. Moore and K. Teter (2014) “Group-effort applied research: Expanding opportunities for undergraduate research through original, class-based research projects.” Biochem Mol Biol Educ. 2014 Jul 8;42(4):331-8. PMID: 24898007.
  2. A. Naganathan and S.D. Moore (2013) “Crippling the essential GTPase Der causes dependence on ribosomal protein L9.” J Bacteriol. 2013 Aug;195(16):3682-91. PMID: 23772068.
  3. A.C. Carr, K.L. Taylor, M.S. Osborne, B.T. Belous, J.P. Myerson, and S.D. Moore (2012) “Rapid depletion of target proteins allows identification of coincident physiological responses.” J Bacteriol. 2012 Nov;194(21):5932-40. PMID: 22942249.
  4. A.C. Carr and S. D. Moore (2012) “Robust quantification of polymerase chain reactions using global fitting.” PLoS One 7(5):e37640.  PMID: 22701526.

For more publication information, please visit Pubmed.

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