COUPLING OF OPEN READING FRAMES BY TRANSLATIONAL BYPASSING
Translational bypassing joins the information found within two disparate open reading frames into a single polypeptide chain. The underlying mechanism centers on the decoding properties of peptidyl-transfer RNA (tRNA) and involves three stages: take-off, scanning, and landing. In take-off, the pepti...
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Published in | Annual review of biochemistry Vol. 69; no. 1; pp. 343 - 372 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Palo Alto, CA 94303-0139
Annual Reviews
01.01.2000
4139 El Camino Way, P.O. Box 10139 Annual Reviews, Inc USA |
Subjects | |
Online Access | Get full text |
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Summary: | Translational bypassing joins the information found within two disparate
open reading frames into a single polypeptide chain. The underlying mechanism
centers on the decoding properties of peptidyl-transfer RNA (tRNA) and involves
three stages: take-off, scanning, and landing. In take-off, the
peptidyl-tRNA/messenger RNA (mRNA) complex in the P site of the ribosome
dissociates, and the mRNA begins to move through the ribosome. In scanning, the
peptidyl-tRNA probes the mRNA sliding through the decoding center. In landing,
the peptidyl-tRNA re-pairs with a codon with which it can form a stable
interaction. Although few examples of genes are known that rely on
translational bypassing to couple open reading frames, ribosomes appear to have
an innate capacity for bypassing. This suggests that the strategy of
translational bypassing may be more common than presently appreciated. The best
characterized example of this phenomenon is T4 gene
60
, in which a
complex set of signals stimulates bypassing of 50 nucleotides between the two
open reading frames. In this review, we focus on the bypassing mechanism of
gene
60
in terms of take-off, scanning, and landing. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Article-1 ObjectType-Feature-3 ObjectType-Review-2 |
ISSN: | 0066-4154 1545-4509 |
DOI: | 10.1146/annurev.biochem.69.1.343 |