Structure of Human Mitochondrial Translation Initiation Factor 3 Bound to the Small Ribosomal Subunit.

ABSTRACT: The human mitochondrial translational initiation factor 3 (IF3_mt) carries mitochondrial-specific amino acid extensions at both its N and C termini (N- and C-terminal extensions [NTE and CTE, respectively]), when compared with its eubacterial counterpart. Here we present 3.3- to 3.5-Å-resolution cryoelectron microscopic structures of the mammalian 28S mitoribosomal subunit in complex with human IF3_mt. Unique contacts observed between the 28S subunit and N-terminal domain of IF3_mt explain its unusually high affinity for the 28S subunit, whereas the position of the mito-specific NTE suggests NTE's role in binding of initiator tRNA to the 28S subunit. The location of the C-terminal domain (CTD) clarifies its anti-association activity, whereas the orientation of

SUBMITTER: Koripella RK 

PROVIDER: S-EPMC6352543 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature