One protein from two open reading frames: mechanism of a 50 nt translational bypass
AUTOR(ES)
Herr, Alan J.
FONTE
Oxford University Press
RESUMO
Translating ribosomes bypass a 50 nt coding gap in order to fuse the information found in the two open reading frames (ORFs) of bacteriophage T4 gene 60. This study investigates the underlying mechanism by focusing on the competition between initiation of bypassing and termination at the end of the first ORF. While nearly all ribosomes initiate bypassing, no more than 50% resume translation in the second ORF. Two previously described cis-acting stimulatory signals are critical for favoring initiation of bypassing over termination. Genetic analysis of these signals supports a working model in which the first (a stem–loop structure at the junction between the first ORF and the coding gap) interferes with decoding in the A-site, and the second (a stretch of amino acids in the nascent peptide encoded by the first ORF) destabilizes peptidyl-tRNA–mRNA pairing.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=212773Documentos Relacionados
- Translational Control of Protein Kinase Cη by Two Upstream Open Reading Frames ▿
- Resistance of Human Cytomegalovirus to Benzimidazole Ribonucleosides Maps to Two Open Reading Frames: UL89 and UL56
- Selecting Open Reading Frames From DNA
- Physical evidence for distinct mechanisms of translational control by upstream open reading frames
- A novel multicopy suppressor of a groEL mutation includes two nested open reading frames transcribed from different promoters.