Fate of a Synthetic Polynucleotide Directing Cell-Free Protein Synthesis II. Association with Ribosomes

Tritiated-poly U, when added to cell-free extracts of Escherichia coli, became associated with ribosomes. This association occurred at 3°C and did not require high-energy phosphate compounds. Small amounts of tritiated polyuridylic acid produced polydisperse ribosomal aggregates with sedimentation c...

Full description

Saved in:
Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 138; no. 3542; pp. 813 - 817
Main Authors Barondes, Samuel H., Nirenberg, Marshall W.
Format Journal Article
LanguageEnglish
Published United States American Association for the Advancement of Science 16.11.1962
Subjects
Acetates
Adjectives
Centrifugation
Magnesium
Messenger RNA
Modeling
Molecules
Protein synthesis
Ribosomes
RNA
Online AccessGet full text

Cover

More Information
Summary:Tritiated-poly U, when added to cell-free extracts of Escherichia coli, became associated with ribosomes. This association occurred at 3°C and did not require high-energy phosphate compounds. Small amounts of tritiated polyuridylic acid produced polydisperse ribosomal aggregates with sedimentation constants of approximately 100 to 130. C$^{14}$-phenylalanine initially was incorporated into protein only on these particles, which suggests that they are the sites of polyphenylalanine synthesis.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0036-8075
1095-9203
DOI:10.1126/science.138.3542.813