Abstract:
:Escherichia coli 50 S ribosomal subunits were reconstituted with and without protein L16 present. The latter particles, although active in puromycin reaction, were unable to use CACCA-Phe as an acceptor substrate. We also found that L16 interacts directly with this oligonucleotide and, in the complex with tRNA, protects its 3'-end from pancreatic ribonuclease digestion. We suggest that the role of L16 is in the fixation of the aminoacyl stem of tRNA to the ribosome at its A-site.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Maimets T,Remme J,Villems Rdoi
10.1016/0014-5793(84)80043-5subject
Has Abstractpub_date
1984-01-23 00:00:00pages
53-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(84)80043-5journal_volume
166pub_type
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