Identification and characterization of protein N-myristoylation occurring on four human mitochondrial proteins, SAMM50, TOMM40, MIC19, and MIC25
| Autor: | Takuro Hosokawa, Toshihiko Utsumi, Ayane Tanikawa, Hirotsugu Kobuchi, Aoi Otsuka, Kanako Matsuzaki, Koko Moriya, Yuki Kikkawa, Aya Kiwado, Yoshihito Iuchi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Mitochondrial intermembrane space Cell Membranes Protein Expression lcsh:Medicine Mitochondrion Biochemistry Physical Chemistry Myristic Acid 0302 clinical medicine Mitochondrial Precursor Protein Import Complex Proteins lcsh:Science Integral membrane protein Energy-Producing Organelles Multidisciplinary Chemistry Cell biology Mitochondria Precipitation Techniques Molecular Mass Physical Sciences lipids (amino acids peptides and proteins) Metabolic Labeling Cell fractionation Cellular Structures and Organelles Bacterial outer membrane Research Article Immunoprecipitation Bioenergetics Research and Analysis Methods Mitochondrial Proteins 03 medical and health sciences Gene Expression and Vector Techniques Animals Humans Integral Membrane Proteins Amino Acid Sequence Molecular Biology Techniques Molecular Biology Molecular Biology Assays and Analysis Techniques lcsh:R Biology and Life Sciences Membrane Proteins Membrane Transport Proteins Cell Biology Outer Membrane Proteins 030104 developmental biology Membrane protein Chemical Properties Gene Expression Regulation Cell Labeling lcsh:Q Lipid modification Protein Processing Post-Translational 030217 neurology & neurosurgery |
| Zdroj: | PLoS ONE PLoS ONE, Vol 13, Iss 11, p e0206355 (2018) |
| ISSN: | 1932-6203 |
| Popis: | Previously, we showed that SAMM50, a mitochondrial outer membrane protein, is N-myristoylated, and this lipid modification is required for the proper targeting of SAMM50 to mitochondria. In this study, we characterized protein N-myristoylation occurring on four human mitochondrial proteins, SAMM50, TOMM40, MIC19, and MIC25, three of which are components of the mitochondrial intermembrane space bridging (MIB) complex, which plays a critical role in the structure and function of mitochondria. In vitro and in vivo metabolic labeling experiments revealed that all four of these proteins were N-myristoylated. Analysis of intracellular localization of wild-type and non-myristoylated G2A mutants of these proteins by immunofluorescence microscopic analysis and subcellular fractionation analysis indicated that protein N-myristoylation plays a critical role in mitochondrial targeting and membrane binding of two MIB components, SAMM50 and MIC19, but not those of TOMM40 and MIC25. Immunoprecipitation experiments using specific antibodies revealed that MIC19, but not MIC25, was a major N-myristoylated binding partner of SAMM50. Immunoprecipitation experiments using a stable transformant of MIC19 confirmed that protein N-myristoylation of MIC19 is required for the interaction between MIC19 and SAMM50, as reported previously. Thus, protein N-myristoylation occurring on two mitochondrial MIB components, SAMM50 and MIC19, plays a critical role in the mitochondrial targeting and protein-protein interaction between these two MIB components. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |