Cooperativity in Low-affinity Mg2+ Binding to tRNA*
作者： D Labuda , K Nicoghosian , R Cedergren
DOI: 10.1016/S0021-9258(20)71213-5
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摘要: Abstract The Pb2+-catalyzed cleavage of tRNAPhe has been used to probe the effect Na+ and Mg2+ binding tRNA. is a noncompetitive inhibitor cleavage. Millimolar also inhibitor. Analysis data show that at least two sites are involved in there an interaction between (cooperativity). Low-affinity thus different from "weak" "strong" tRNA characterized previously. We postulate alterations induced by low-affinity mimic some extent those brought about RNA with protein factor appropriate [Mg2+] whole structure able respond concerted way signal environment such as aminoacylation or codon binding.
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