A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase

Autor: Trevor Lithgow, Renae Allen, Traude H. Beilharz, Billie Egan, Kip Gabriel
Předmět:
Saccharomyces cerevisiae Proteins
Proline
Macromolecular Substances
Translocase of the outer membrane
Recombinant Fusion Proteins
Green Fluorescent Proteins
Molecular Sequence Data
Biophysics
TIM/TOM complex
Saccharomyces cerevisiae
Protein targeting
Biology
medicine.disease_cause
Biochemistry
Mitochondrial Membrane Transport Proteins
Fungal Proteins
Structural Biology
Mitochondrial Precursor Protein Import Complex Proteins
Genetics
medicine
Molecular Biology
Integral membrane protein
Conserved Sequence
Sequence Homology
Amino Acid

Peripheral membrane protein
Membrane Proteins
Membrane Transport Proteins
Cell Biology
Intracellular Membranes
Transmembrane protein
Cell biology
Mitochondria
Luminescent Proteins
Protein Subunits
Translocase of the inner membrane
Intermembrane space
Carrier Proteins
Protein Binding
Zdroj: Monash University
Popis: The TOM translocase consists of several integral membrane proteins organised around the channel forming protein Tom40. Here we show that one of these protein subunits, Tom7, is a tail-anchored protein. The carboxy-terminal 33 amino acids of Tom7 contain the information for targeting the protein to the mitochondrial outer membrane, and a conserved proline residue within the transmembrane segment is required for efficient targeting of Tom7 to the outer membrane. An equivalent proline residue is important in targeting each of the other three tail-anchored proteins that associate with Tom40 to form the core of the TOM translocase.
Databáze: OpenAIRE