Abstract
The DNA-directed synthesis of beta-galactosidase in Escherichia coli extracts has been investigated in a partially fractionated system. A dependency was obtained for 3',5'-cyclic AMP receptor protein and also for a factor, from the salt wash of ribosomes, that has been purified to near homogeneity. This factor has been identified with a ribosome release factor previously purified from the supernatant fraction by A. Hirashima and A. Kaji [(1972) Biochemistry 11,4037-4044]. In the coupled transcription-translation system this factor stimulates beta-galactosidase synthesis and total protein synthesis 2- to 4-fold. It is thus clear that the ribosome release factor has a physiological function in translation. It may also affect transcription, because it stimulated total RNA synthesis up to 50% in this in vitro system.
MeSH Terms
Cross Reactions
DNA, Bacterial/metabolism
Escherichia coli/enzymology
Galactosidases/biosynthesis
Immunodiffusion
Kinetics
Molecular Weight
Peptide Chain Termination, Translational
Polyribosomes/metabolism
Protein Biosynthesis
RNA, Messenger/metabolism
Receptors, Cyclic AMP/metabolism
Ribosomal Proteins/isolation & purification,metabolism
Transcription, Genetic
beta-Galactosidase/biosynthesis
Chemicals
DNA, Bacterial
RNA, Messenger
Receptors, Cyclic AMP
Ribosomal Proteins
Galactosidases
beta-Galactosidase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kung H F
Treadwell B V
Spears C
Tai P C
Weissbach H
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30 references, click to expand
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