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TitleStructural insights into unique features of the human mitochondrial ribosome recycling.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 17, Page 8283-8288, Year 2019
Publish dateApr 23, 2019
AuthorsRavi K Koripella / Manjuli R Sharma / Paul Risteff / Pooja Keshavan / Rajendra K Agrawal /
PubMed AbstractMammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with ...Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with bacteria, the composition and structure of the human mitoribosome and its translational factors are significantly different from those of their bacterial counterparts. The mammalian mitoribosome recycling factor (RRF) carries a mito-specific N terminus extension (NTE), which is necessary for the function of RRF Here we present a 3.9-Å resolution cryo-electron microscopic (cryo-EM) structure of the human 55S mitoribosome-RRF complex, which reveals α-helix and loop structures for the NTE that makes multiple mito-specific interactions with functionally critical regions of the mitoribosome. These include ribosomal RNA segments that constitute the peptidyl transferase center (PTC) and those that connect PTC with the GTPase-associated center and with mitoribosomal proteins L16 and L27. Our structure reveals the presence of a tRNA in the pe/E position and a rotation of the small mitoribosomal subunit on RRF binding. In addition, we observe an interaction between the pe/E tRNA and a mito-specific protein, mL64. These findings help understand the unique features of mitoribosome recycling.
External linksProc Natl Acad Sci U S A / PubMed:30962385 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 4.4 Å
Structure data

0514

6nu2

EMDB-0514, PDB-6nu2:
Structural insights into unique features of the human mitochondrial ribosome recycling
Method: EM (single particle) / Resolution: 3.9 Å

0515

6nu3

EMDB-0515, PDB-6nu3:
Structural insights into unique features of the human mitochondrial ribosome recycling
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • Human (human)
KeywordsRIBOSOME / mitochondrial ribosome recycling Factor / mtRRF / 55S

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