Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli.
نویسندگان
چکیده
The universal genetic code includes three codons which signal polypeptide chain termination. These termination or nonsense codons are UAG (amber), UAA (ochre), and UGA (opal). Usually, Escherichia coli and other procaryotic cells do not contain transfer ribonucleic acids (tRNAs) which recognize these codons. However, such tRNAs can be created by suppressor mutations in tRNA genes, generating tRNAs with the ability to recognize termination codons. Most suppressor mutations are located in the anticodon triplet and alter it to CUA, UUA, or UCA, the characteristic anticodons in amber, ochre, and opal suppressor tRNAs, respectively. Whereas amber suppressor tRNAs only recognize amber codons, tRNAs with ochre anticodons (UUA) recognize both ochre and amber codons, and at least some tRNAs with opal anticodons (UCA) recognize UGG tryptophan codons in addition to opal codons. Because of the involvement of tRNA in this process, termination suppression (also called nonsense suppression) is part of the larger topic of "informational suppression" (77). Other mechanisms of tRNA-mediated informational suppression include missense suppression and frameshift suppression. These will not be discussed in this review. Research on missense suppression has been thoroughly
منابع مشابه
Wobble decoding by the Escherichia coli selenocysteine insertion machinery
Selenoprotein expression in Escherichia coli redefines specific single UGA codons from translational termination to selenocysteine (Sec) insertion. This process requires the presence of a Sec Insertion Sequence (SECIS) in the mRNA, which forms a secondary structure that binds a unique Sec-specific elongation factor that catalyzes Sec insertion at the predefined UGA instead of release factor 2-m...
متن کاملA bacterial strain with a unique quadruplet codon specifying non-native amino acids.
The addition of noncanonical amino acids to the genetic code requires unique codons not assigned to the 20 canonical amino acids. Among the 64 triplet codons, only the three nonsense "stop" codons have been used to encode non-native amino acids. Use of quadruplet "frame-shift" suppressor codons provides an abundant alternative but suffers from low suppression efficiency as a result of competing...
متن کاملSuppression of glutamic acid codons by mutant glycine transfer ribonucleic acid.
In previous mutational studies with mutant trpA46 (Gly [GGA] --> Glu [GAA] at position 211 of the tryptophan synthetase alpha chain) of Escherichia coli, no missense suppressors were detected. Such suppressors have now been obtained by single mutations in gly Vins, the structural gene for a GGA/G-reading, mutationally altered form of gly V transfer ribonucleic acid (tRNA) (tRNA(Gly) which reads...
متن کاملPleiotropic phenotype of an Escherichia coli mutant lacking leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase.
A mutant of Escherichia coli that lacks leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase had diminished activities of L-phenylalanyl-transfer ribonucleic acid synthetase and tryptophanase, grew faster than its parent with aspartic acid as the sole nitrogen source, accumulated higher levels of enterochelin in the medium during iron limitation, and exhibited an abnormal morphol...
متن کاملTetracycline-regulated suppression of amber codons in mammalian cells.
As an approach to inducible suppression of nonsense mutations in mammalian cells, we described recently an amber suppression system in mammalian cells dependent on coexpression of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) along with the E. coli glutamine-inserting amber suppressor tRNA. Here, we report on tetracycline-regulated expression of the E. coli GlnRS gene and, thereby, tetrac...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Microbiological reviews
دوره 52 3 شماره
صفحات -
تاریخ انتشار 1988