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pubmed-article:19383686pubmed:dateCreated2009-6-2lld:pubmed
pubmed-article:19383686pubmed:abstractTextIn Escherichia coli homocysteine (Hcy) is metabolically converted to the thioester Hcy-thiolactone in ATP-consuming reactions catalysed by methionyl-, isoleucyl- and leucyl-tRNA synthetases. Here we show that growth inhibition caused by supplementation of E. coli cultures with Hcy is accompanied by greatly increased accumulation of Hcy-thiolactone. Energy dissipation for Hcy editing increases 100-fold in the presence of exogenous Hcy and reaches one mole of ATP unproductively dissipated for Hcy-thiolactone synthesis per each mole of ATP that is consumed for methionine activation. Inhibiting Hcy-thiolactone synthesis with isoleucine, leucine or methionine accelerates bacterial growth in Hcy-supplemented cultures. Growth rates in Hcy-inhibited cultures are inversely related to the accumulation of Hcy-thiolactone. We also show that the levels of protein N-linked Hcy modestly increase in E. coli cells in Hcy-supplemented cultures. The results suggest that Hcy editing restrains bacterial growth.lld:pubmed
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pubmed-article:19383686pubmed:year2009lld:pubmed
pubmed-article:19383686pubmed:articleTitleHomocysteine editing and growth inhibition in Escherichia coli.lld:pubmed
pubmed-article:19383686pubmed:affiliationDepartment of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, International Center for Public Health, Newark, NJ 07101, USA.lld:pubmed
pubmed-article:19383686pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19383686pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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