Eileen Ambing

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A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB)(More)
Introduction. Transcriptional regulators play a crucial role in the adaptation of microorganisms to diverse environmental challenges. 1–3 Most microbial transcriptional regulators contain an effector binding regulatory domain and a DNA-binding domain that interacts with a specific operator DNA to either prevent (transcriptional repress-ors) or stimulate(More)
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