Abstract：
:In vitro transcription by T7 RNA polymerase was used to prepare 32 different mutations in the 21 nucleotides that participate in the 9 tertiary base pairs or triples of yeast tRNAPhe. The mutations were designed either to disrupt the tertiary interaction or to change the sequence without disrupting the structure by transplanting tertiary interactions present in other tRNAs. Steady-state aminoacylation kinetics with purified yeast phenylalanyl synthetase revealed little change in reaction rate as long as a tertiary interaction was maintained. This suggests that the tertiary nucleotides only contribute to the folding of tRNAPhe and do not participate directly in sequence-specific interaction with the synthetase.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Sampson JR,DiRenzo AB,Behlen LS,Uhlenbeck OCdoi
10.1021/bi00462a014subject
Has Abstractpub_date
1990-03-13 00:00:00pages
2523-32issue
10eissn
0006-2960issn
1520-4995journal_volume
29pub_type
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