Preferential binding of isoaccepting species of tRNALys and tRNAIle from lupin cotyledons to polyribosomes.
Polyribosome-bound and -unbound isoaccepting species of tRNALys and tRNAIle, isolated from lupin cotyledons, were compared by RPC-5 chromatography and it was found that polyribosomes preferentially bind some of the isoaccepting species. The preference in binding of given isoacceptors changes with the age of lupin seedling. The results suggest that the tRNALys species recognising the same codons can affect the rate of translation in lupin cotyledons.
D003062:Codon / Q000378:metabolism; D007532:Isoleucine; D008239:Lysine; D010944:Plants / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D013997:Time Factors
D003062:Codon; D012346:RNA, Transfer, Amino Acyl; D007532:Isoleucine; D008239:Lysine