Open AccessMitoribosomal small subunit maturation involves formation of initiation-like complexes
Author(s) -
Tea Lenarčič,
Moritz Niemann,
D.J.F. Ramrath,
Salvatore Calderaro,
Timo Flügel,
Martin Saurer,
Marc Leibundgut,
Daniel Boehringer,
C. Prange,
Elke K. Horn,
André Schneider,
Nenad Ban
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2114710118
Subject(s) - mitochondrial ribosome , biology , protein subunit , ribosome , microbiology and biotechnology , eukaryotic small ribosomal subunit , ribosomal protein , initiation factor , ribosomal rna , mitochondrion , inner mitochondrial membrane , biochemistry , gene , rna
Significance Mitochondria originated from ancestral bacteria and they still maintain their own reduced genome and translational apparatus that feature highly diverged mitoribosomes, specialized for the synthesis of membrane proteins. Only recently, high-resolution cryo-EM structures of the mature mitoribosomes from several species revealed their unusual structural features. Nevertheless, the mechanisms of their assembly are relatively poorly understood. To better understand how mitoribosomes are assembled and which factors participate in this process, we investigated assembly intermediates of the small mitoribosomal subunit fromTrypanosoma brucei to reveal that the process involves a modular stepwise exchange of assembly factors that facilitate the formation of the functional decoding center of the small ribosomal subunit, and we discovered that mitochondrial initiation factor 2 participates in this process.