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@ARTICLE{Khawaja:878079,
author = {Khawaja, Anas and Itoh, Yuzuru and Remes, Cristina and
Spåhr, Henrik and Yukhnovets, Olessya and Höfig, Henning
and Amunts, Alexey and Rorbach, Joanna},
title = {{D}istinct pre-initiation steps in human mitochondrial
translation},
journal = {Nature Communications},
volume = {11},
number = {1},
issn = {2041-1723},
address = {[London]},
publisher = {Nature Publishing Group UK},
reportid = {FZJ-2020-02621},
pages = {2932},
year = {2020},
abstract = {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 mammal},
cin = {IBI-6},
ddc = {500},
cid = {I:(DE-Juel1)IBI-6-20200312},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:32522994},
UT = {WOS:000543969100003},
doi = {10.1038/s41467-020-16503-2},
url = {https://juser.fz-juelich.de/record/878079},
}