Reconstitution of a Minimal Small Ribosomal Subunit

1993 ◽  
pp. 719-726 ◽  
Author(s):  
Andrew Scheinman ◽  
Anna-Marie Aguinaldo ◽  
Agda M. Simpson ◽  
Marian Peris ◽  
Gary Shankweiler ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Small Ribosomal Subunit

scholarly journals Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis

2013 ◽  
Vol 110 (38) ◽  
pp. 15253-15258 ◽  
Author(s):  
U. A. Hellmich ◽  
B. L. Weis ◽  
A. Lioutikov ◽  
J. P. Wurm ◽  
M. Kaiser ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Ribosomal Subunit ◽  
Ribosome Assembly ◽  
Small Ribosomal Subunit ◽  
Assembly Factor

Primary structure of protein S13 from the small ribosomal subunit ofEscherichia coli

FEBS Letters ◽  
1976 ◽  
Vol 71 (2) ◽  
pp. 251-255 ◽  
Author(s):  
Harald Lindemann ◽  
Brigitte Wittmann-Liebold
Keyword(s):  
Primary Structure ◽  
Ribosomal Subunit ◽  
Ofescherichia Coli ◽  
Small Ribosomal Subunit

scholarly journals Structural Aspects of RbfA Action during Small Ribosomal Subunit Assembly

2007 ◽  
Vol 28 (3) ◽  
pp. 434-445 ◽  
Author(s):  
Partha P. Datta ◽  
Daniel N. Wilson ◽  
Masahito Kawazoe ◽  
Neil K. Swami ◽  
Tatsuya Kaminishi ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Small Ribosomal Subunit ◽  
Subunit Assembly ◽  
Structural Aspects

scholarly journals The modifying enzyme Tsr3 establishes the hierarchy of Rio kinase activity in 40S ribosome assembly

2021 ◽  
Author(s):  
Haina Huang ◽  
Melissa Parker ◽  
Katrin Karbstein
Keyword(s):  
Quality Control ◽  
Binding Site ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Kinase Activity ◽  
Ribosomal Subunit ◽  
Ribosome Assembly ◽  
Small Ribosomal Subunit ◽  
Yeast Strains

AbstractRibosome assembly is an intricate process, which in eukaryotes is promoted by a large machinery comprised of over 200 assembly factors (AF) that enable the modification, folding, and processing of the ribosomal RNA (rRNA) and the binding of the 79 ribosomal proteins. While some early assembly steps occur via parallel pathways, the process overall is highly hierarchical, which allows for the integration of maturation steps with quality control processes that ensure only fully and correctly assembled subunits are released into the translating pool. How exactly this hierarchy is established, in particular given that there are many instances of RNA substrate “handover” from one highly related AF to another remains to be determined. Here we have investigated the role of Tsr3, which installs a universally conserved modification in the P-site of the small ribosomal subunit late in assembly. Our data demonstrate that Tsr3 separates the activities of the Rio kinases, Rio2 and Rio1, with whom it shares a binding site. By binding after Rio2 dissociation, Tsr3 prevents rebinding of Rio2, promoting forward assembly. After rRNA modification is complete, Tsr3 dissociates, thereby allowing for recruitment of Rio1. Inactive Tsr3 blocks Rio1, which can be rescued using mutants that bypass the requirement for Rio1 activity. Finally, yeast strains lacking Tsr3 randomize the binding of the two kinases, leading to the release of immature ribosomes into the translating pool. These data demonstrate a role for Tsr3 and its modification activity in establishing a hierarchy for the function of the Rio kinases.

scholarly journals Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Cell ◽  
2000 ◽  
Vol 102 (5) ◽  
pp. 615-623 ◽  
Author(s):  
Frank Schluenzen ◽  
Ante Tocilj ◽  
Raz Zarivach ◽  
Joerg Harms ◽  
Marco Gluehmann ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Small Ribosomal Subunit

scholarly journals On the stoichiometry of proteins in the small ribosomal subunit of hepatoma ascites cells

FEBS Letters ◽  
1976 ◽  
Vol 62 (2) ◽  
pp. 132-135 ◽  
Author(s):  
P. Westermann ◽  
W. Heumann ◽  
H. Bielka
Keyword(s):  
Ribosomal Subunit ◽  
Small Ribosomal Subunit
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