A reduced level of charged tRNAArgmnm5UCU triggers the wild-type peptidyl-tRNA to frameshift

Leipuviene, Ramune; Björk, Glenn R.

doi:10.1261/rna.7256705

Cited by 10 publications

(12 citation statements)

References 76 publications

(85 reference statements)

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“…Since the sufF44 mutation was not located in an area of the chromosome where any of the glycine tRNA genes are located, the sufF gene was suggested to encode a tRNA modification enzyme (264,265). However, it was later shown to be mutated in the argU gene, which codes for tRNA mnm5UCU Arg (179). The alterations in tRNA mnm5UCU Arg cause instability or less-efficient arginylation, resulting in a decreased concentration of charged tRNA mnm5UCU Arg .…”

Section: The Classic Set Of Suppressors Isolated As Revertants Of Salmentioning

confidence: 99%

A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment

Atkins

Björk

2009

Microbiol Mol Biol Rev

131

126

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SUMMARYMutants of translation components which compensate for both −1 and +1 frameshift mutations showed the first evidence for framing malleability. Those compensatory mutants isolated in bacteria and yeast with altered tRNA or protein factors are reviewed here and are considered to primarily cause altered P-site realignment and not altered translocation. Though the first sequenced tRNA mutant which suppressed a +1 frameshift mutation had an extra base in its anticodon loop and led to a textbook “yardstick” model in which the number of anticodon bases determines codon size, this model has long been discounted, although not by all. Accordingly, the reviewed data suggest that reading frame maintenance and translocation are two distinct features of the ribosome. None of the −1 tRNA suppressors have anticodon loops with fewer than the standard seven nucleotides. Many of the tRNA mutants potentially affect tRNA bending and/or stability and can be used for functional assays, and one has the conserved C74 of the 3′ CCA substituted. The effect of tRNA modification deficiencies on framing has been particularly informative. The properties of some mutants suggest the use of alternative tRNA anticodon loop stack conformations by individual tRNAs in one translation cycle. The mutant proteins range from defective release factors with delayed decoding of A-site stop codons facilitating P-site frameshifting to altered EF-Tu/EF1α to mutant ribosomal large- and small-subunit proteins L9 and S9. Their study is revealing how mRNA slippage is restrained except where it is programmed to occur and be utilized.

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Section: The Classic Set Of Suppressors Isolated As Revertants Of Salmentioning

confidence: 99%

A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment

Atkins

Björk

2009

Microbiol Mol Biol Rev

131

126

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“…The hisC3072 mutant contains a G insertion in a run of G's: GGG GAA AGA (NNN) 29 UGA [presented as the zero frame following the insertion; the inserted G is underlined, and (NNN) 29 stands for (25). External suppressors rendering the hisC3072 mutant able to grow without addition of histidine were selected.…”

Section: Resultsmentioning

confidence: 99%

“…The sequences of hisD3018 (26), hisC3737 (4), hisD3749 (3), hisD6610 (26), and hisC3072 (25) were determined earlier. The frameshift suppressor sufA codes for altered tRNA CGG Pro , the sufB codes for altered tRNA GGG Pro , the sufD codes for altered tRNA CCC Gly , and the sufF codes for altered tRNA mnm 5 UCU Arg were published previously (22,25,34,36,39). b ϩ and (ϩ), stronger or weaker growth observed after 3 days or earlier; -, no growth after 4 days; ND, not determined.…”

Section: Discussionmentioning

confidence: 99%

“…One class of mutants obtained by such a selection was defective in tRNA mnm 5 UCU Arg , resulting in either a reduced concentration of the tRNA or a reduced arginylation of it. It was proposed that inefficient decoding of the AGA codon by the defective tRNA mnm 5 UCU Arg stalls the ribosome at the A-site codon, allowing the wild-type form of the peptidyl tRNA mnm 5 s 2 UCU Glu to slip forward one nucleotide and thereby reestablish the ribosome in the zero frame (25). Another class of ϩ1 frameshift suppressor mutants, which are analyzed here, shows that the ribosomal 50S subunit protein L9 plays an important role in reading frame maintenance, in support of earlier observations (15).…”

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confidence: 99%

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Alterations in the Two Globular Domains or in the Connecting α-Helix of Bacterial Ribosomal Protein L9 Induces +1 Frameshifts

Leipuviene

Björk

2007

J Bacteriol

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The ribosomal 50S subunit protein L9, encoded by the gene rplI, is an elongated protein with an ␣-helix connecting the N-and C-terminal globular domains. We isolated rplI mutants that suppress the ؉1 frameshift mutation hisC3072 in Salmonella enterica serovar Typhimurium. These mutants have amino acid substitutions in the N-terminal domain (G24D) or in the C-terminal domain (I94S, A102D, G126V, and F132S) of L9. In addition, different one-base deletions in rplI altered either the final portion of the C terminus or removed the C-terminal domain with or without the connecting ␣-helix. An alanine-to-proline substitution at position 59 (A59P), which breaks the ␣-helix between the globular domains, induced ؉1 frameshifting, suggesting that the geometrical relationship between the N and C domains is important to maintain the reading frame. Except for the alterations G126V in the C terminus and A59P in the connecting ␣-helix, our results confirm earlier results obtained by using the phage T4 gene 60-based system to monitor bypassing. The way rplI mutations suppress various frameshift mutations suggests that bypassing of many codons from several takeoff and landing sites occurred instead of a specific frameshift forward at overlapping codons.

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“…The presence of these codons, alone or in tandem, close to the initiation codon was reported to negatively regulate protein synthesis (Chen and Inouye, 1994;Olivares-Trejo et al, 2003;Yoon and Walter, 2007). Moreover, the diminished quantity of the tRNA cognate for AGA or an alteration of its spatial structure, could induce a +1 frameshifting at a single AGA codon (Leipuviene and Bjork, 2005).…”

Section: Introductionmentioning

confidence: 99%

Ribosome can resume the translation in both +1 or −1 frames after encountering an AGA cluster in Escherichia coli

Lainé¹,

Thouard²,

Komar³

et al. 2008

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A reduced level of charged tRNA^Arg_mnm⁵UCU triggers the wild-type peptidyl-tRNA to frameshift

Cited by 10 publications

References 76 publications

A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment

A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment

Alterations in the Two Globular Domains or in the Connecting α-Helix of Bacterial Ribosomal Protein L9 Induces +1 Frameshifts

Ribosome can resume the translation in both +1 or −1 frames after encountering an AGA cluster in Escherichia coli

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