scholarly journals Dipeptide-Based Models of Nickel Superoxide Dismutase: Solvent Effects Highlight a Critical Role to Ni–S Bonding and Active Site Stabilization

2011 ◽  
Vol 50 (20) ◽  
pp. 10460-10471 ◽  
Author(s):  
Eric M. Gale ◽  
Darin M. Cowart ◽  
Robert A. Scott ◽  
Todd C. Harrop
2014 ◽  
Vol 20 (21) ◽  
pp. 6283-6286 ◽  
Author(s):  
Chien-Wei Chiang ◽  
Yun-Li Chu ◽  
Hong-Ling Chen ◽  
Ting-Shen Kuo ◽  
Way-Zen Lee

2021 ◽  
Author(s):  
Tea Lenarcic ◽  
Mateusz Jaskolowski ◽  
Marc Leibundgut ◽  
Alain Scaiola ◽  
Tanja Schoenhut ◽  
...  

Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. Structural basis of the mammalian mitochondrial ribosome assembly is currently not understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving 7 assembly factors. We discover that NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by MRM2 methyltransferase and quality control interactions with a conserved mitochondrial GTPase MTG2 that contacts the sarcin ricin loop and the immature active site. The successive action of these factors leads to the formation of the peptidyl transferase active site of the mitoribosome and the folding of the surrounding rRNA regions responsible for interactions with tRNAs and the small ribosomal subunit.


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