Biological Activity of Escherichia coli tRNAPhe Modified in Its C-C-A Terminus
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چکیده
منابع مشابه
Cellular location and activity of Escherichia coli RecG proteins shed light on the function of its structurally unresolved C-terminus
RecG is a DNA translocase encoded by most species of bacteria. The Escherichia coli protein targets branched DNA substrates and drives the unwinding and rewinding of DNA strands. Its ability to remodel replication forks and to genetically interact with PriA protein have led to the idea that it plays an important role in securing faithful genome duplication. Here we report that RecG co-localises...
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Nucleoside base modifications can alter the structures and dynamics of RNA molecules and are important in tRNAs for maintaining translational fidelity and efficiency. The unmodified anticodon stem-loop from Escherichia coli tRNA(Phe) forms a trinucleotide loop in solution, but Mg2+ and dimethylallyl modification of A37 N6 destabilize the loop-proximal base pairs and increase the mobility of the...
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متن کاملThe crystal structure of unmodified tRNAPhe from Escherichia coli
Post-transcriptional nucleoside modifications fine-tune the biophysical and biochemical properties of transfer RNA (tRNA) so that it is optimized for participation in cellular processes. Here we report the crystal structure of unmodified tRNA(Phe) from Escherichia coli at a resolution of 3 A. We show that in the absence of modifications the overall fold of the tRNA is essentially the same as th...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1972
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1972.tb01935.x