Faculty Opinions recommendation of Kinetics and mechanism of mammalian mitochondrial ribosome assembly.

Author(s):  
Alexey Amunts
Cell Reports ◽  
2018 ◽  
Vol 22 (7) ◽  
pp. 1935-1944 ◽  
Author(s):  
Daniel F. Bogenhagen ◽  
Anne G. Ostermeyer-Fay ◽  
John D. Haley ◽  
Miguel Garcia-Diaz

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.


Cell Reports ◽  
2016 ◽  
Vol 16 (7) ◽  
pp. 1874-1890 ◽  
Author(s):  
Oliver Rackham ◽  
Jakob D. Busch ◽  
Stanka Matic ◽  
Stefan J. Siira ◽  
Irina Kuznetsova ◽  
...  

PLoS Genetics ◽  
2020 ◽  
Vol 16 (7) ◽  
pp. e1008923 ◽  
Author(s):  
Aurelio Reyes ◽  
Paola Favia ◽  
Sara Vidoni ◽  
Vittoria Petruzzella ◽  
Massimo Zeviani

1982 ◽  
Vol 24 (6) ◽  
pp. 741-759 ◽  
Author(s):  
A. Rieck ◽  
A. J. F. Griffiths ◽  
H. Bertrand

From a sample of 122 natural isolates of Neurospora intermedia collected recently from around the world, five variants had erratic stop-start growth patterns reminiscent of the phenotype of "stopper" laboratory extranuclear mutants of Neurospora crassa. Like laboratory isolated mutants, the natural "stopper" variants were sterile as protoperithecial parents and transmitted the variant growth phenotypes very inefficiently, if at all, as male parents. Heterokaryon tests could not be made because of strain incompatibilities. Four of the variants have mitochondrial cytochrome aa3 and b deficiencies. These four variants are all defective in mitochondrial ribosome assembly and have abnormal ratios of large to small subunits. Restriction enzyme analyses revealed some similarity of N. intermedia to N. crassa mtDNA. One normal and four variant strains had additional DNA in comparison to a standard normal strain. Cumulatively, the results indicate that the genetic alterations which cause stopper phenotypes of these natural isolates of N. intermedia are of mitochondrial rather than nuclear origin.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Tea Lenarčič ◽  
Mateusz Jaskolowski ◽  
Marc Leibundgut ◽  
Alain Scaiola ◽  
Tanja Schönhut ◽  
...  

AbstractMitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. The structural basis of the mammalian mitochondrial ribosome assembly is currently not well understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving seven assembly factors. We discover that the 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 the MRM2 methyltransferase and quality control interactions with the 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.


Cell Reports ◽  
2018 ◽  
Vol 23 (1) ◽  
pp. 127-142 ◽  
Author(s):  
Kara L. Perks ◽  
Giulia Rossetti ◽  
Irina Kuznetsova ◽  
Laetitia A. Hughes ◽  
Judith A. Ermer ◽  
...  

1979 ◽  
Vol 177 (1) ◽  
pp. 73-84 ◽  
Author(s):  
Richard A. Collins ◽  
Helmut Bertrand ◽  
Robert J. LaPolla ◽  
Alan M. Lambowitz

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