Identification and characterization of signal peptide of Mitofusin1 (Mfn1)

Biochem Biophys Res Commun. 2019 Feb 12;509(3):707-712. doi: 10.1016/j.bbrc.2018.12.165. Epub 2019 Jan 8.

Abstract

Mitofusin1 (Mfn1) mediates outer mitochondrial membrane (OMM) fusion in Opisthokonts. The uncharacterized TM comprises to two helices (namely, the TM1 and TM2) connected by an intermembrane loop. Consistent with previous studies, our results from in silico analyses show that all mitofusins lack N terminal-MTS and the TM may act an internal MTS. We have identified a conserved region in TM domain that is responsible for mitochondrial localization of Mfn1/2. Thus, our results suggest the dual function of TM; in OMM anchoring and signaling Mfn1 to mitochondria. Our study illuminates the underlying role of TM for mitochondrial localization of Mfn1 on one hand and also paves a way for the development of tools for in silico prediction of cellular localization of proteins.

Keywords: Internal MTS; Mitofusins (Mfn1 and Mfn2); N-Terminal mitochondrial targeting sequence (MTS); Signal peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism*
  • Humans
  • Mitochondria / metabolism
  • Mitochondrial Membrane Transport Proteins / chemistry
  • Mitochondrial Membrane Transport Proteins / metabolism*
  • Mitochondrial Membranes / metabolism*
  • Protein Conformation, alpha-Helical
  • Protein Domains
  • Protein Sorting Signals*

Substances

  • Mitochondrial Membrane Transport Proteins
  • Protein Sorting Signals
  • GTP Phosphohydrolases
  • Mfn1 protein, human