1989
DOI: 10.1016/0022-2836(89)90385-9
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Translation of phage f1 gene VII occurs from an inherently defective initiation site made functional by coupling

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Cited by 45 publications
(53 citation statements)
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“…Indeed, this site seems to lack the features required for independent recognition by ribosomes. Such a translational coupling mechanism has been shown to be required for the synthesis of gene VII in the f1 filamentous bacteriophage (15,16). Thus, TolQ controls the expression of TolR at a translational level.…”
Section: Discussionmentioning
confidence: 99%
“…Indeed, this site seems to lack the features required for independent recognition by ribosomes. Such a translational coupling mechanism has been shown to be required for the synthesis of gene VII in the f1 filamentous bacteriophage (15,16). Thus, TolQ controls the expression of TolR at a translational level.…”
Section: Discussionmentioning
confidence: 99%
“…In systems where reinitiation plays a role, the same ribosome that completes translation of the upstream gene is then captured (usually with low efficiency) for initiation of translation of the coupled gene. 25,26 Reinitiation may be necessitated by the existence of a weak SD sequence or other sequence constraints in the intergenic region. [26][27][28][29][30] In some coupled systems, both mechanisms are known to play a role.…”
Section: Introductionmentioning
confidence: 99%
“…However, it has been observed that translation of some genes in a polycistronic mRNA is dependent on the translation of a contiguous upstream gene. This interdependence of translation efficiency of neighboring genes, called translational coupling, is used in phage and bacteria to regulate expression of some proteins (Ivey-Hoyle and Steege, 1989). In E. coli, translational coupling has been observed for genes encoding ribosomal proteins (Lindahl et al, 1989;Lindahl and Zengel, 1986) and genes trpBA (Aksoy et al, 1984), trpDE (Oppenheim and Yanofsky, 1980) and galKT (Schumperli et al, 1982).…”
Section: Introductionmentioning
confidence: 96%