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Structure paper

TitleDistinct pre-initiation steps in human mitochondrial translation.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 2932, Year 2020
Publish dateJun 10, 2020
AuthorsAnas Khawaja / Yuzuru Itoh / Cristina Remes / Henrik Spåhr / Olessya Yukhnovets / Henning Höfig / Alexey Amunts / Joanna Rorbach /
PubMed AbstractTranslation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two ...Translation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two distinct mitochondrial pre-initiation assembly steps involving those factors. Single-particle cryo-EM revealed that in the first step, interactions between mitochondria-specific protein mS37 and mtIF3 keep the small mitoribosomal subunit in a conformation favorable for a subsequent accommodation of mtIF2 in the second step. Combination with fluorescence cross-correlation spectroscopy analyses suggests that mtIF3 promotes complex assembly without mRNA or initiator tRNA binding, where exclusion is achieved by the N-terminal and C-terminal domains of mtIF3. Finally, the association of large mitoribosomal subunit is required for initiator tRNA and leaderless mRNA recruitment to form a stable initiation complex. These data reveal fundamental aspects of mammalian protein synthesis that are specific to mitochondria.
External linksNat Commun / PubMed:32522994 / PubMed Central
MethodsEM (single particle)
Resolution2.85 - 3.38 Å
Structure data

10021

6rw4

EMDB-10021, PDB-6rw4:
Structure of human mitochondrial 28S ribosome in complex with mitochondrial IF3
Method: EM (single particle) / Resolution: 2.97 Å

10022

6rw5

EMDB-10022, PDB-6rw5:
Structure of human mitochondrial 28S ribosome in complex with mitochondrial IF2 and IF3
Method: EM (single particle) / Resolution: 3.14 Å

EMDB-10023:
Mitochondrial 28S ribosome with IF3 (masked refined the body core)
Method: EM (single particle) / Resolution: 2.87 Å

EMDB-10024:
Mitochondrial 28S ribosome with IF3 (masked refined the head core)
Method: EM (single particle) / Resolution: 2.85 Å

EMDB-10025:
Mitochondrial 28S ribosome with IF3 (masked refined the tail)
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-10026:
Mitochondrial 28S ribosome with IF3 (masked refined mS39)
Method: EM (single particle) / Resolution: 3.04 Å

EMDB-10027:
Mitochondrial 28S ribosome with IF3 (masked refined IF3)
Method: EM (single particle) / Resolution: 2.85 Å

EMDB-10028:
Mitochondrial 28S ribosome with IF2 and IF3 (masked refined the body core)
Method: EM (single particle) / Resolution: 3.02 Å

EMDB-10029:
Mitochondrial 28S ribosome with IF2 and IF3 (masked refined the head core)
Method: EM (single particle) / Resolution: 3.02 Å

EMDB-10030:
Mitochondrial 28S ribosome with IF2 and IF3 (masked refined the tail)
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-10031:
Mitochondrial 28S ribosome with IF2 and IF3 (masked refined mS39)
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-10032:
Mitochondrial 28S ribosome with IF2 and IF3 (masked refined IF2 and IF3-CTD)
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide

ChemComp-SPM:
SPERMINE / Spermine

ChemComp-SRY:
STREPTOMYCIN / medication, antibiotic*YM / Streptomycin

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM / 5'-Guanylyl imidodiphosphate

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsRIBOSOME / ribosomal small subunit / initiation complex / initiation factor 3 / mitochondria / initiation factor

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