Chemistry and Biochemistry

John C. Price

John Price

Office: BNSN E113
Office Phone: 801-422-6040
Lab Room: BNSN E180
Email: jcprice@chem.byu.edu
Office Hours

Education:

BS Chemistry, Utah State University (2001)

PhD Biochemistry and Molecular Biology, Pennslyvania State University (2005)

Postdoctoral Fellow studying Prion Biology with Stanley Prusiner, University of California, San Francisco (2005-2010)

Curriculum Vitae

Research:

Price Lab Group

  My research explores mechanisms used by living cells to control the synthesis and degradation of protein.  Specifically, we use mass spectrometry and stable isotopes to label newly synthesized molecules with a time dependent tag.  This allows us to measure both in vivo concentrations, and replacement rate. With a mass spectrometer, the time-dependent stable isotope enrichment can be measured in any molecule of a complex mixture, allowing us to monitor large numbers of proteins simultaneously and perform experiments that survey broad sections of the proteome.  We have successfully used this technique in many different biosynthetic systems from "cell free" environments to humans (see Figure and Figure Legend).

    Currently, we are focused on understanding post-transcriptional control of the proteome composition within cells, focusing on the use of stored mRNA and protein degradation

Post-transcriptional control of cell metabolism using stored mRNA. Multiple processes critical to human health are known to employ stored mRNA, yet these systems are difficult to investigate using current tools.  The mRNA is present in the cell for an indefinite period of time before signal dependent translation of the specific protein occurs.  By following signal specific protein synthesis we can approach the understanding of these systems from the "bottom up" to identify the biochemical pathways activated within the cell.

Maintenance of proteome homeostasis through protein catabolism.  Many of today’s most devastating diseases can be identified as diseases of protein homeostasis.  Parkinson’s, Alzheimer’s, Huntington’s, diabetes and other diseases all exhibit cellular deposits of aggregated protein.  These aggregates are often highly resistant to degradation and may indicate a dysfunction within the catabolic machinery of the cell.  Continuous protein catabolism is critical in the presence of constitutive transcription and translation, yet these processes are poorly understood.  It has recently been shown that the cell employs thousands of proteins, (ubiquitin ligases, targeted proteases, proteasome, etc.) to guide the process of protein degradation.  Thus, the complexity of the regulatory structure for removing a protein from the cell may be comparable to producing the protein in the first place.  Our current work is focused on identifying the substrates for cellular proteases and understanding how targeted proteolytic processing is used by the cell.

Publications:

1. Louie KB, Bowen BP, McAlhany S, Huang Y, Price JC, Mao JM, Hellerstein MK, Northen TR, 2013 “In
situ kinetic histochemistry” Nature Scientific Reports, 3:1656, DOI: 10.1038/srep01656


2. Price JC, Khambatta CF, Li KW, Bruss MD, Shankaran M, Dalidd M, Floreani NA, Roberts LS, Turner
SM, Holmes WE, and Hellerstein MK, 2012 “The effect of long‐term calorie restriction on hepatic
proteostasis and mitochondrial dynamics in mice” Mol. Cell. Proteomics, 11.12, pg: 1801‐1814


3. Krebs C, Dassama LMK, Matthews ML, Jiang W, Price JC, Korboukh V, Li N, Bollinger JM Jr. 2012
”Novel approaches for the accumulation of oxygenated intermediates to multi‐millimolar
concentrations” Coordination Chemistry Reviews, 257, pg: 234‐243


4. Guan S, Price JC, Gheammaghami S, Prusiner SB, Burlingame AL, 2012 “Compartment Modeling
for mammalian protein turnover studies by stable isotope metabolic labeling” Ana Chem.,
84(9):4014‐21


5. Price JC, Holmes WE, Li KW, Floreani NA, Neese RA, Turner SM, Hellerstein MK, 2011
“Measurement of human plasma proteome dynamics with 2H2O and liquid chromatography
tandem mass spectrometry.” Ana. Biochem., 420(1):73‐83

See CV above for full list.