Ribosomal protein L16 binds to the 3'-end of transfer RNA.

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 Lett

journal_title

FEBS letters

authors

Maimets T,Remme J,Villems R

doi

10.1016/0014-5793(84)80043-5

subject

Has Abstract

pub_date

1984-01-23 00:00:00

pages

53-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)80043-5

journal_volume

166

pub_type

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