Normal tRNAs promote ribosomal frameshifting
- Cold Spring Harbor Lab., NY
The addition of SER/sup AGU//sub AGC/ tRNA to an E. coli cell-free protein synthesizing system which contains the endogenous tRNA levels results in up to 100% of the ribosomes translating the MS2 coat gene shifting into the -1 reading frame. An analogous phenomenon is seen at a much lower level without the tRNA addition, where a shift into the +1 frame can also be detected. Thus translation with the endogenous tRNA levels yields proteins which have the amino terminus of the coat protein but which are substantially larger than the coat protein and comprise about 5% of the coat translation. Since the lysis gene overlaps the 3' end of the coat gene in the +1 frame, it is concluded that the reading frame shift into the +1 frame yields a hybrid protein. Also, evidence is presented that ribosomes translating the synthetase gene shift into the -1 frame near the distal end of the gene. This frameshifting is promoted by thr/sup ACU//sub ACC/ tRNA. Specific competitor tRNAs for both Thr and Ser tRNA-promoted frameshifting have been characterized. The generality of this new mechanism for producing additional proteins is unclear, but its investigation should increase understanding of the coding mechanism and its origin.
- OSTI ID:
- 6530590
- Journal Information:
- Cell; (United States), Vol. 18
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
RIBOSOMES
MOLECULAR STRUCTURE
TRANSFER RNA
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
BIOLOGICAL PATHWAYS
BIOSYNTHESIS
CODONS
ESCHERICHIA COLI
GENETIC EFFECTS
GENETICS
PROTEINS
SERINE
THREONINE
TRANSCRIPTION
VIRUSES
AMINO ACIDS
BACTERIA
BIOLOGICAL EFFECTS
BIOLOGY
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CHEMISTRY
HYDROXY ACIDS
KINETICS
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANOIDS
PARASITES
REACTION KINETICS
RNA
SYNTHESIS
550400* - Genetics
550700 - Microbiology
550200 - Biochemistry