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Growth of Escherichia coli DL41(DE3) in enhanced chemically defined media in the presence of L‐telluromethionine (778.7)
Author(s) -
Cooper Brent,
Taylor Savannah,
Broderick Kathleen,
Boles Jeffrey
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.778.7
Subject(s) - escherichia coli , methionine , amino acid , biochemistry , chemistry , auxotrophy , biology , gene
In analyzing the three‐dimensional structure of a protein, the x‐ray crystallography endeavor can be improved by incorporating unnatural amino acids into that protein. Most naturally occurring atoms do not have sufficient mass to diffract electrons. Using unnatural amino acids containing a metalloid provides a solution to this problem. Bioincorporation of L‐Telluromethionine can provide residues with sufficient mass for electron scattering when incorporated serendipitously. However telluromethionine has cytotoxic effects which reduce cell growth and uptake. A proteomic analysis of telluromethionyl Escherichia coli was carried out using the methionine auxotroph E. collie DL41(DE3) (pCock) expression system. Both telluromethionyl and methionyl exposed cultures were analyzed with the objective of identifying differentially expressed proteins. The biological roles of differentially expressed proteins was elucidated and have been applied to improving methods for the bioincorporation of telluromethionine via the supplementation of chemically defined media with metabolites that were negatively affected due to the exposure to L‐Telluromethionine.