Mitochondrial ribosome assembly in Neurospora crassa: Mutants with defects in mitochondrial ribosome assembly

1979 ◽  
Vol 177 (1) ◽  
pp. 73-84 ◽  
Author(s):  
Richard A. Collins ◽  
Helmut Bertrand ◽  
Robert J. LaPolla ◽  
Alan M. Lambowitz
1977 ◽  
Vol 116 (2) ◽  
pp. 189-205 ◽  
Author(s):  
Robert J. LaPolla ◽  
Alan M. Lambowitz

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 ◽  
...  

1976 ◽  
Vol 18 (3) ◽  
pp. 397-409 ◽  
Author(s):  
H. Bertrand ◽  
N. A. Szakacs ◽  
F. E. Nargang ◽  
C. A. Zagozeski ◽  
R. A. Collins ◽  
...  

The 18 extranuclear mutants of Neurospora crassa, without exception, have abnormal mitochondrial respiratory systems. On the basis of genetic, phenotypic and physiological criteria, these mutants are divided into four groups: 1) the cytochrome aa3 and b deficient "poky" variants that are defective in mitochondrial ribosome assembly, 2) the cytochrome aa3 deficient mutants, [mi-3] and [exn-5], that appear to have genetic lesions affecting a component of a regulatory system controlling cytochrome aa3 synthesis, 3) the cytochrome aa3 and b deficient "stopper" mutants with physiological lesions that probably affect mitochondrial protein synthesis, and 4) cni-3, a mutant that is constitutive for an inducible mitochondrial cyanide-insensitive oxidase in spite of having a normal cytochrome mediated electron-transport system. It is proposed that the mitochondrial genophore not only codes for cellular components that are essential for the formation of the mitochondrial protein synthesizing apparatus, but also for components of a regulatory system that coordinates the expression of nuclear and mitochondrial genes during the biogenesis of the mitochondrial electron-transport system.


2020 ◽  
Vol 8 (8) ◽  
pp. 1186
Author(s):  
Adrien Beau Desaulniers ◽  
Nishka Kishore ◽  
Kelly Adames ◽  
Frank E. Nargang

The Neurospora crassa AOD1 protein is a mitochondrial alternative oxidase that passes electrons directly from ubiquinol to oxygen. The enzyme is encoded by the nuclear aod-1 gene and is produced when the standard electron transport chain is inhibited. We previously identified eleven strains in the N. crassa single gene deletion library that were severely deficient in their ability to produce AOD1 when grown in the presence of chloramphenicol, an inhibitor of mitochondrial translation that is known to induce the enzyme. Three mutants affected previously characterized genes. In this report we examined the remaining mutants and found that the deficiency of AOD1 was due to secondary mutations in all but two of the strains. One of the authentic mutants contained a deletion of the yvh1 gene and was found to have a deficiency of aod-1 transcripts. The YVH1 protein localized to the nucleus and a post mitochondrial pellet from the cytoplasm. A zinc binding domain in the protein was required for rescue of the AOD1 deficiency. In other organisms YVH1 is required for ribosome assembly and mutants have multiple phenotypes. Lack of YVH1 in N. crassa likely also affects ribosome assembly leading to phenotypes that include altered regulation of AOD1 production.


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.


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