Mitochondrial translation release factor 1 like (MTRF1L)

Mitochondrial translation release factor 1 like (MTRF1L) is a mitochondrial protein that directs the termination of mitochondrial translation by recognizing and acting upon the standard stop codons UAA and UAG, thereby promoting peptide chain release from the ribosome[3][4][6]. It functions as a release factor in the translation termination of mitochondrially encoded proteins, ensuring proper dissociation of the newly synthesized protein from the ribosome, tRNA, and mRNA[3][6]. MTRF1L's action is essential for the synthesis of functional mitochondrial proteins involved in oxidative phosphorylation, and it shares sequence similarity with bacterial release factors[3]. Mutations or functional deficiencies in MTRF1L may contribute to diseases such as spastic ataxia and alcoholic gastritis[3]. The protein acts specifically on UAA/UAG codons, as the mitochondrial genetic code interprets UGA as tryptophan, and MTRF1L does not have activity on non-cognate stop codons AGA and AGG in vitro[3][6]. Other mitochondrial release factors, such as mtRF1, instead function at non-standard stop codons including AGA and AGG[1][3]. Alternative splicing of the MTRF1L gene may result in multiple transcript variants[3]. While not a current target of any approved drugs and lacking established biomarker or therapeutic safety concerns, its central role in mitochondrial protein synthesis termination makes it an important molecule in the study of mitochondrial biology and disease[3][4][6].

Other names

Peptide chain release factor 1-like, mitochondrialMTRF1LMTRF1AHMRF1LmtRF1aMitochondrial translational release factor 1-likeMRF1L