Mitochondrial translation elongation

Stable Identifier
Homo sapiens
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Translation elongation proceeds by cycles of aminoacyl-tRNAs binding, peptide bond formation, and displacement of deacylated tRNAs (reviewed in Christian and Spremulli 2012). In each cycle an aminoacyl-tRNA in a complex with TUFM:GTP (EF-Tu:GTP) binds a cognate codon at the A-site of the ribosome, GTP is hydrolyzed, and TUFM:GDP dissociates. The elongating polypeptide bonded to the tRNA at the P-site is transferred to the aminoacyl group at the A-site by peptide bond formation, leaving a deacylated tRNA at the P-site and the elongating polypeptide attached to the tRNA at the A-site. GFM1:GTP (EF-Gmt:GTP) binds, GTP is hydrolyzed, GFM1:GDP dissociates, and the ribosome translocates 3 nucleotides in the 3' direction, relocating the peptidyl-tRNA to the P-site and allowing another cycle to begin. Mitochondrial ribosomes associate with the inner membrane and polypeptides are co-translationally inserted into the membrane (reviewed in Ott and Herrmann 2010, Agrawal and Sharma 2012). TUFM:GDP is regenerated to TUFM:GTP by the guanine nucleotide exchange factor TSFM (EF-Ts, EF-TsMt).

Literature References
PubMed ID Title Journal Year
19962410 Co-translational membrane insertion of mitochondrially encoded proteins

Ott, M, Herrmann, JM

Biochim. Biophys. Acta 2010
22959417 Structural aspects of mitochondrial translational apparatus

Agrawal, RK, Sharma, MR

Curr. Opin. Struct. Biol. 2012
22172991 Mechanism of protein biosynthesis in mammalian mitochondria

Spremulli, LL, Christian, BE

Biochim. Biophys. Acta 2012
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