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Journal Article

Cloning and expression of the metE gene in Escherichia coli

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Shoeman,  Robert L.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/0003986185907131/pdf?md5=e103cebc9496be456da8f80e05fa2998&pid=1-s2.0-0003986185907131-main.pdf
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https://doi.org/10.1016/0003-9861(85)90713-1
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Citation

Chu, J., Shoeman, R. L., Hart, J., Coleman, T., Mazaitis, A., Kelker, N., et al. (1985). Cloning and expression of the metE gene in Escherichia coli. Archives of Biochemistry and Biophysics, 239(2), 467-474. doi:10.1016/0003-9861(85)90713-1.


Cite as: https://hdl.handle.net/21.11116/0000-0000-CF1F-6
Abstract
A lambda-transducing phage was isolated that contains the metE gene. This gene codes for N5-methyl-H4-folate:homocysteine methyltransferase (EC 2.1.1.14), an enzyme that catalyzes the terminal reaction in methionine biosynthesis. A 9.1-kb EcoR1 fragment of this phage, containing the metE gene, was then cloned into pBR325. This plasmid, pJ19, was used to transform Escherichia coli strain 2276, a metE mutant, and restore the MetE+ phenotype. Although the transformed cells produced large amounts of the metE protein in vivo, in vitro studies using pJ19 as template showed low synthesis of the metE protein.