scholarly journals Cryo-EM structure of yeast 90S preribosome at 3.4 Å resolution

2020 ◽  
Author(s):  
Yifei Du ◽  
Weidong An ◽  
Keqiong Ye
Keyword(s):  
18S Rrna ◽  
Ribosomal Subunit ◽  
Small Ribosomal Subunit ◽  
Central Domain ◽  
Closed Conformation ◽  
Open Conformation ◽  
Assembly Mechanism ◽  
High Resolution Structure ◽  
Assembly Intermediate ◽  
Resolution Structure

AbstractPreviously, we determined a cryo-EM structure of Saccharomyces cerevisiae 90S preribosome obtained after depletion of the RNA helicase Mtr4 at 4.5 Å resolution (Sun et al., 2017). The 90S preribosome is an early assembly intermediate of small ribosomal subunit. Here, the structure was improved to 3.4 Å resolution and reveals many previously unresolved structures and interactions, in particular around the central domain of 18S rRNA. The central domain adopts a closed conformation in our structure, in contrast to an open conformation in another high-resolution structure of S. cerevisiae 90S. The new model of 90S would serve as a better reference for investigation of the assembly mechanism of small ribosomal subunit.

scholarly journals High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Cell ◽  
2001 ◽  
Vol 107 (5) ◽  
pp. 679-688 ◽  
Author(s):  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Anat Bashan ◽  
Sharon Gat ◽  
...  
Keyword(s):  
High Resolution ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
High Resolution Structure ◽  
Resolution Structure

What we have learned from ribosome structures

2008 ◽  
Vol 36 (4) ◽  
pp. 567-574 ◽  
Author(s):  
V. Ramakrishnan
Keyword(s):  
High Resolution ◽  
Ribosomal Subunit ◽  
Ribosomal Subunits ◽  
30S Subunit ◽  
High Resolution Structure ◽  
70S Ribosome ◽  
Year 2000 ◽  
Resolution Structure

The determination of the high-resolution structures of ribosomal subunits in the year 2000 and of the entire ribosome a few years later are revolutionizing our understanding of the role of the ribosome in translation. In the present article, I summarize the main contributions from our laboratory to this worldwide effort. These include the determination of the structure of the 30S ribosomal subunit and its complexes with antibiotics, the role of the 30S subunit in decoding, and the high-resolution structure of the entire 70S ribosome complexed with mRNA and tRNA.

scholarly journals Posttranscriptional down-regulation of small ribosomal subunit proteins correlates with reduction of 18S rRNA in RPS19 deficiency

FEBS Letters ◽  
2009 ◽  
Vol 583 (12) ◽  
pp. 2049-2053 ◽  
Author(s):  
Jitendra Badhai ◽  
Anne-Sophie Fröjmark ◽  
Hamid Reza Razzaghian ◽  
Edward Davey ◽  
Jens Schuster ◽  
...  
Keyword(s):  
18S Rrna ◽  
Ribosomal Subunit ◽  
Down Regulation ◽  
Small Ribosomal Subunit

scholarly journals The complete structure of the small subunit processome

2017 ◽  
Author(s):  
Jonas Barandun ◽  
Malik Chaker-Margot ◽  
Mirjam Hunziker ◽  
Kelly R. Molloy ◽  
Brian T. Chait ◽  
...  
Keyword(s):  
Ribosomal Proteins ◽  
18S Rrna ◽  
Molecular Mimicry ◽  
Ribosomal Subunit ◽  
Small Subunit ◽  
Ribosome Assembly ◽  
Complete Structure ◽  
Small Ribosomal Subunit ◽  
Rna Remodeling ◽  
Rrna Cleavage

The small subunit processome represents the earliest stable precursor of the eukaryotic small ribosomal subunit. Here we present the cryo-EM structure of the Saccharomyces cerevisiae small subunit processome at an overall resolution of 3.8 Å, which provides an essentially complete atomic model of this assembly. In this nucleolar superstructure, 51 ribosome assembly factors and two RNAs encapsulate the 18S rRNA precursor and 15 ribosomal proteins in a state that precedes pre-rRNA cleavage at site A1. Extended flexible proteins are employed to connect distant sites in this particle. Molecular mimicry, steric hindrance as well as protein-and RNA-mediated RNA remodeling are used in a concerted fashion to prevent the premature formation of the central pseudoknot and its surrounding elements within the small ribosomal subunit.

Variable region V1 of Saccharomyces cerevisiae 18S rRNA participates in biogenesis and function of the small ribosomal subunit

Chromosoma ◽  
1997 ◽  
Vol 105 (7-8) ◽  
pp. 523-531
Author(s):  
Rob W. van Nues ◽  
Jaap Venema ◽  
Rudi J. Planta ◽  
Hendrik A. Raué
Keyword(s):  
Saccharomyces Cerevisiae ◽  
18S Rrna ◽  
Ribosomal Subunit ◽  
Variable Region ◽  
Small Ribosomal Subunit ◽  
And Function

High-resolution structure of human phosphoserine phosphatase in open conformation

2003 ◽  
Vol 59 (6) ◽  
pp. 971-977 ◽  
Author(s):  
Yves Peeraer ◽  
Anja Rabijns ◽  
Christel Verboven ◽  
Jean-François Collet ◽  
Emile Van Schaftingen ◽  
...  
Keyword(s):  
High Resolution ◽  
Phosphoserine Phosphatase ◽  
Open Conformation ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals METTL15 interacts with the assembly intermediate of murine mitochondrial small ribosomal subunit to form m4C840 12S rRNA residue

2020 ◽  
Vol 48 (14) ◽  
pp. 8022-8034 ◽  
Author(s):  
Ivan Laptev ◽  
Ekaterina Shvetsova ◽  
Sergey Levitskii ◽  
Marina Serebryakova ◽  
Maria Rubtsova ◽  
...  
Keyword(s):  
Protein Biosynthesis ◽  
Mitochondrial Protein ◽  
Ribosomal Subunit ◽  
12S Rrna ◽  
Small Ribosomal Subunit ◽  
Mitochondrial Ribosomes ◽  
Murine Cell Line ◽  
Assembly Factor ◽  
Mitochondrial 12S Rrna ◽  
Assembly Intermediate

Abstract Mammalian mitochondrial ribosomes contain a set of modified nucleotides, which is distinct from that of the cytosolic ribosomes. Nucleotide m4C840 of the murine mitochondrial 12S rRNA is equivalent to the dimethylated m4Cm1402 residue of Escherichia coli 16S rRNA. Here we demonstrate that mouse METTL15 protein is responsible for the formation of m4C residue of the 12S rRNA. Inactivation of Mettl15 gene in murine cell line perturbs the composition of mitochondrial protein biosynthesis machinery. Identification of METTL15 interaction partners revealed that the likely substrate for this RNA methyltransferase is an assembly intermediate of the mitochondrial small ribosomal subunit containing an assembly factor RBFA.

scholarly journals A Local Role for the Small Ribosomal Subunit Primary Binder rpS5 in Final 18S rRNA Processing in Yeast

PLoS ONE ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. e10194 ◽  
Author(s):  
Andreas Neueder ◽  
Steffen Jakob ◽  
Gisela Pöll ◽  
Jan Linnemann ◽  
Rainer Deutzmann ◽  
...  
Keyword(s):  
18S Rrna ◽  
Ribosomal Subunit ◽  
Rrna Processing ◽  
Small Ribosomal Subunit
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