ArticleNucleic acids research2009
The amino terminal domain from Mrt4 protein can functionally replace the RNA binding domain of the ribosomal P0 protein.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 47 citations in OpenAlex.
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- Mutational Analyses of the Cysteine-Rich Domain of Yvh1, a Protein Required for Translational Competency in Yeast.Biology · 2022Article
- The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.Nucleic acids research · 2022Article
- Recombinant expression and biophysical characterization of Mrt4 protein that involved in mRNA turnover and ribosome assembly fromBioengineered · 2022Article
- The ribosome assembly factor Nop53 has a structural role in the formation of nuclear pre-60S intermediates, affecting late maturation events.Nucleic acids research · 2021Article
- Pollen Number and Ribosome Gene Expression Altered in a Genome-Editing Mutant ofFrontiers in plant science · 2021Article
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- Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae.Nucleic acids research · 2018Article
- MoYvh1 subverts rice defense through functions of ribosomal protein MoMrt4 in Magnaporthe oryzae.PLoS pathogens · 2018Article
- Puf3 participates in ribosomal biogenesis in malaria parasites.Journal of cell science · 2018Article
- Molecular basis of the human ribosomopathy Shwachman-Diamond syndrome.Advances in biological regulation · 2018Review
- Screening of potential genes contributing to the macrocycle drug resistance of C. albicans via microarray analysis.Molecular medicine reports · 2017Article
- Placeholder factors in ribosome biogenesis: please, pave my way.Microbial cell (Graz, Austria) · 2017Review
- Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit.Nature structural & molecular biology · 2016Article
- Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy.RNA (New York, N.Y.) · 2016Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, the Mrt4 protein is a component of the ribosome assembly machinery that shares notable sequence homology to the P0 ribosomal stalk protein. Here, we show that these proteins can not bind simultaneously to ribosomes and moreover, a chimera containing the first 137 amino acids of Mrt4 and the last 190 amino acids from P0 can partially complement the absence of the ribosomal protein in a conditional P0 null mutant. This chimera is associated with ribosomes isolated from this strain when grown under restrictive conditions, although its binding is weaker than that of P0. These ribosomes contain less P1 and P2 proteins, the other ribosomal stalk components. Similarly, the interaction of the L12 protein, a stalk base component, is affected by the presence of the chimera. These results indicate that Mrt4 and P0 bind to the same site in the 25S rRNA. Indeed, molecular dynamics simulations using modelled Mrt4 and P0 complexes provide further evidence that both proteins bind similarly to rRNA, although their interaction with L12 displays notable differences. Together, these data support the participation of the Mrt4 protein in the assembly of the P0 protein into the ribosome and probably, that also of the L12 protein.
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