Ultraviolet light-induced crosslinking of two major phosphoproteins and poly(A)+RNA from free polyribosomes; changes in phosphorylation by inhibitors of transcription and translation
Polyribosomes were isolated without the use of detergents, irradiated with ultraviolet light and labelled in the presence of (gamma-/sup 32/P) adenosine 5'-triphosphate. Poly(A)+RNA-protein structures separated by chromatography on oligo (dT)-cellulose contained up to 1o crosslinked proteins as shown by SDS-polyacrylamide gel electrophoresis. These included a 71 kDa poly(A)-bound species and two major phosphoproteins of 66 and 13o kDa. Pretreatment of rats with inhibitors of transcription and translation caused different and significant alterations in the labelling of the two phosphoproteins, suggesting that phosphorylation of proteins closely associated with mRNA may be involved in the regulation of the stability of this RNA or its binding to structural elements in the cell.
- Research Organization:
- Max-Planck-Institut fuer Biochemie, Deutschland, Germany, F.R.
- OSTI ID:
- 5559643
- Journal Information:
- Biochem. Biophys. Res. Commun.; (United States), Vol. 1
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PROTEINS
CROSS-LINKING
PHOSPHORYLATION
ATP
CHROMATOGRAPHY
ELECTROPHORESIS
GENETIC RADIATION EFFECTS
RATS
RIBOSOMES
RNA
TRANSCRIPTION
ULTRAVIOLET RADIATION
ANIMALS
BIOLOGICAL EFFECTS
BIOLOGICAL RADIATION EFFECTS
CELL CONSTITUENTS
CHEMICAL REACTIONS
ELECTROMAGNETIC RADIATION
GENETIC EFFECTS
MAMMALS
NUCLEIC ACIDS
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANOIDS
POLYMERIZATION
RADIATION EFFECTS
RADIATIONS
RODENTS
SEPARATION PROCESSES
VERTEBRATES
560111* - Radiation Effects on Biochemicals- In Vitro- (-1987)