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Abstract
WE have studied the relationship between structure and function of a tRNA by investigating the behaviour of two structurally defined fragments of the molecule. We first describe the properties of an isolated nonadecanucleotide fragment from the E. coli initiator tRNA, tRNAFmet. We show that this fragment, which contains the proposed anticodon CAU and a segment of paired bases, is specifically bound to ribosomes in the presence of the initiator triplets, ApUpG and GpUpG (refs. 1 and 2). We then show that an undecanucleotide fragment, which contains the anticodon but not a segment of paired bases, is not so bound.
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