Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.
Asc1/RACK1 promotes the translation of mRNAs associated with the translational closed loop complex, which have short open reading frames and encode proteins required for core metabolic processes.
TNF-α treatment induces phosphorylation and cytoplasmic translocation of the retinoblastoma protein, which regulates cytoskeletal organization in skeletal muscle cells.
Mitochondria can tune the protein synthesis of nuclear-encoded proteins through condition-dependent mRNA localization that is regulated by translation elongation and the geometric constraints of the cell.
The complex process of protein translocation across membranes has been dissected into multiple key steps and the distributions of translocation rates indicate stochastic nature of the reaction.
A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.