scholarly journals Hierarchical RNA Processing Is Required for Mitochondrial Ribosome Assembly

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

scholarly journals Initial Steps in RNA Processing and Ribosome Assembly Occur at Mitochondrial DNA Nucleoids

2014 ◽  
Vol 19 (4) ◽  
pp. 618-629 ◽  
Author(s):  
Daniel F. Bogenhagen ◽  
Dwight W. Martin ◽  
Antonius Koller
Keyword(s):  
Mitochondrial Dna ◽  
Rna Processing ◽  
Ribosome Assembly

scholarly journals Stepwise maturation of the peptidyl transferase region of human mitoribosomes

2021 ◽  
Author(s):  
Tea Lenarcic ◽  
Mateusz Jaskolowski ◽  
Marc Leibundgut ◽  
Alain Scaiola ◽  
Tanja Schoenhut ◽  
...  
Keyword(s):  
Quality Control ◽  
16S Rrna ◽  
Active Site ◽  
Critical Role ◽  
Ribosomal Subunit ◽  
Structural Basis ◽  
Ribosome Assembly ◽  
Peptidyl Transferase ◽  
Mitochondrial Ribosomes ◽  
Mitochondrial Ribosome

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.

scholarly journals MRM2 and MRM3 are involved in biogenesis of the large subunit of the mitochondrial ribosome

2014 ◽  
Vol 25 (17) ◽  
pp. 2542-2555 ◽  
Author(s):  
Joanna Rorbach ◽  
Pierre Boesch ◽  
Payam A. Gammage ◽  
Thomas J. J. Nicholls ◽  
Sarah F. Pearce ◽  
...  
Keyword(s):  
16S Rrna ◽  
Rna Processing ◽  
Large Subunit ◽  
Peptidyl Transferase ◽  
Mitochondrial Translation ◽  
Peptidyl Transferase Center ◽  
Mitochondrial Ribosome ◽  
Translation Apparatus ◽  
Rrna Maturation ◽  
And Function

Defects of the translation apparatus in human mitochondria are known to cause disease, yet details of how protein synthesis is regulated in this organelle remain to be unveiled. Ribosome production in all organisms studied thus far entails a complex, multistep pathway involving a number of auxiliary factors. This includes several RNA processing and modification steps required for correct rRNA maturation. Little is known about the maturation of human mitochondrial 16S rRNA and its role in biogenesis of the mitoribosome. Here we investigate two methyltransferases, MRM2 (also known as RRMJ2, encoded by FTSJ2) and MRM3 (also known as RMTL1, encoded by RNMTL1), that are responsible for modification of nucleotides of the 16S rRNA A-loop, an essential component of the peptidyl transferase center. Our studies show that inactivation of MRM2 or MRM3 in human cells by RNA interference results in respiratory incompetence as a consequence of diminished mitochondrial translation. Ineffective translation in MRM2- and MRM3-depleted cells results from aberrant assembly of the large subunit of the mitochondrial ribosome (mt-LSU). Our findings show that MRM2 and MRM3 are human mitochondrial methyltransferases involved in the modification of 16S rRNA and are important factors for the biogenesis and function of the large subunit of the mitochondrial ribosome.

scholarly journals RCC1L (WBSCR16) isoforms coordinate mitochondrial ribosome assembly through their interaction with GTPases

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

MITOCHONDRIAL VARIANTS OF NEUROSPORA INTERMEDIA FROM NATURE

1982 ◽  
Vol 24 (6) ◽  
pp. 741-759 ◽  
Author(s):  
A. Rieck ◽  
A. J. F. Griffiths ◽  
H. Bertrand
Keyword(s):  
Genetic Alterations ◽  
Growth Patterns ◽  
Ribosome Assembly ◽  
Normal Strain ◽  
Mitochondrial Cytochrome ◽  
Neurospora Intermedia ◽  
Mitochondrial Ribosome ◽  
The World ◽  
Standard Normal ◽  
Natural Isolates

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.

scholarly journals Stepwise maturation of the peptidyl transferase region of human mitoribosomes

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Tea Lenarčič ◽  
Mateusz Jaskolowski ◽  
Marc Leibundgut ◽  
Alain Scaiola ◽  
Tanja Schönhut ◽  
...  
Keyword(s):  
Quality Control ◽  
16S Rrna ◽  
Active Site ◽  
Critical Role ◽  
Ribosomal Subunit ◽  
Structural Basis ◽  
Ribosome Assembly ◽  
Peptidyl Transferase ◽  
Mitochondrial Ribosomes ◽  
Mitochondrial Ribosome

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.

scholarly journals Kinetics and Mechanism of Mammalian Mitochondrial Ribosome Assembly

Cell Reports ◽  
2018 ◽  
Vol 22 (7) ◽  
pp. 1935-1944 ◽  
Author(s):  
Daniel F. Bogenhagen ◽  
Anne G. Ostermeyer-Fay ◽  
John D. Haley ◽  
Miguel Garcia-Diaz
Keyword(s):  
Kinetics And Mechanism ◽  
Ribosome Assembly ◽  
Mitochondrial Ribosome
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