Structure of the L1 protuberance in the ribosome

Nikulin, Alexei; Eliseikina, I.A.; Tishchenko, Svetlana; Nevskaya, N.; Davydova, Natalia; Platonova, O. V.; Piendl, Wolfgang; Selmer, M.; Liljas, Anders; Drygin, Denis; Zimmermann, Robert A.; Garber, Maria; Nikonov, S.V.

doi:10.1038/nsb886

Cited by 85 publications

(91 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The effects of the rpl1b-1 mutation on CGA read-through might either be due to the general reduction in translating ribosomes known to occur in an rpl1b-Δ mutant (McIntosh et al 2011) or to specific functions of L1 protein. For example, the L1 stalk, to which L1 protein binds, moves significantly during every elongation cycle, interacts with deacylated tRNA (Nikulin et al 2003;Fei et al 2009) and may play a role in the removal of tRNA from the E site (Wilson and Nierhaus 2006). Since ribosomes lacking the L1 protein are competent to translate messages (McIntosh et al 2011), depletion of L1 protein might expedite removal of the tRNA from the E site, which is necessary for binding of the next aminoacyl tRNA in the A site.…”

Section: Discussionmentioning

confidence: 99%

“…We took advantage of a conditional glycerol − phenotype (indicative of a defect in respiration) to clone the gene for one suppressor, which proved to be an allele of RPL1B, a gene that encodes one of two copies of the universally conserved ribosomal protein L1 (Nikulin et al 2003;Fei et al 2008;Cornish et al 2009). Three lines of evidence indicate that the phenotype of this mutant is due to a defect in the RBL1B gene.…”

Section: Read-through Of Cga Codons Is Improved By Treatment With Parmentioning

confidence: 99%

See 1 more Smart Citation

Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1

Letzring

Wolf

Brule

et al. 2013

RNA

112

145

View full text Add to dashboard Cite

Translation of CGA codon repeats in the yeast Saccharomyces cerevisiae is inefficient, resulting in dose-dependent reduction in expression and in production of an mRNA cleavage product, indicative of a stalled ribosome. Here, we use genetics and translation inhibitors to understand how ribosomes respond to CGA repeats. We find that CGA codon repeats result in a truncated polypeptide that is targeted for degradation by Ltn1, an E3 ubiquitin ligase involved in nonstop decay, although deletion of LTN1 does not improve expression downstream from CGA repeats. Expression downstream from CGA codons at residue 318, but not at residue 4, is improved by deletion of either ASC1 or HEL2, previously implicated in inhibition of translation by polybasic sequences. Thus, translation of CGA repeats likely causes ribosomes to stall and exploits known quality control systems. Expression downstream from CGA repeats at amino acid 4 is improved by paromomycin, an aminoglycoside that relaxes decoding specificity. Paromomycin has no effect if native tRNA Arg(ICG) is highly expressed, consistent with the idea that failure to efficiently decode CGA codons might occur in part due to rejection of the cognate tRNA Arg(ICG) . Furthermore, expression downstream from CGA repeats is improved by inactivation of RPL1B, one of two genes encoding the universally conserved ribosomal protein L1. The effects of rpl1b-Δ and of either paromomycin or tRNA Arg(ICG) on CGA decoding are additive, suggesting that the rpl1b-Δ mutant suppresses CGA inhibition by means other than increased acceptance of tRNA Arg(ICG) . Thus, inefficient decoding of CGA likely involves at least two independent defects in translation.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Read-through Of Cga Codons Is Improved By Treatment With Parmentioning

confidence: 99%

Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1

Letzring

Wolf

Brule

et al. 2013

RNA

112

145

View full text Add to dashboard Cite

show abstract

“…3a) [20][21][22]. This binding region in mRNA is built by an asymmetrical internal loop that creates a sharp bend between two helices, thereby resembling the kink-turn motif [3].…”

Section: Recognition Of Three-dimensional Mrna Structures By Proteinsmentioning

confidence: 99%

Towards deciphering the principles underlying an mRNA recognition code

Serganov

Patel

2008

Current Opinion in Structural Biology

View full text Add to dashboard Cite

Messenger RNAs interact with a number of different molecules that determine the fate of each transcript and contribute to the overall pattern of gene expression. These interactions are governed by specific mRNA signals, which in principle could represent a special mRNA recognition 'code'. Both, small molecules and proteins demonstrate a diversity of mRNA binding modes often dependent on the structural context of the regions surrounding specific target sequences. In this review, we have highlighted recent structural studies that illustrate the diversity of recognition principles used by mRNA binders for timely and specific targeting and processing of the message.

show abstract

“…This protuberance is made of only one large protein (L1) anchored to the 28S rRNA and involved in the release of the deacylated tRNA from the exit site (E-site) of the ribosome (Nikulin et al, 2003).…”

Section: Componentsmentioning

confidence: 99%

The puzzling lateral flexible stalk of the ribosome

Gonzalo

Reboud

2003

Biology of the Cell

127

131

View full text Add to dashboard Cite

The lateral flexible stalk of the large ribosomal subunit is made of several interacting proteins anchored to a conserved region of the 28S (26S) rRNA termed the GTPase-associated domain or thiostrepton loop. This structure is demonstrated to adopt puzzling changes of conformation following the different steps of the elongation cycle. Some of these proteins termed the P-proteins in eukaryotes and L10 and L7/L12 in bacteria, present little structural similarities between Eubacteria on one side and Archae and Eukaryotes on the other side. However, up to now, these proteins seem to present a similar macromolecular organisation and they have been involved in the same functions. Convincing evidence attests that these proteins participate in elongation factor binding to the ribosome, and it has been suggested that these proteins might be evolved in a GTP hydrolysis activating protein activity. Involvement of these proteins in the translational mechanism is discussed. Moreover, in eukaryotes, small P-proteins are also found as isolated proteins in a cytoplasmic pool that exchanges with the ribosome-associated P-proteins. Moreover, a part of the ribosomal proteins is phosphorylated (hence their P-protein names). The biological signification of these particularities is discussed.

show abstract

Structure of the L1 protuberance in the ribosome

Cited by 85 publications

References 28 publications

Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1

Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1

Towards deciphering the principles underlying an mRNA recognition code

The puzzling lateral flexible stalk of the ribosome

Contact Info

Product

Resources

About