Protein N-myristoylation plays a critical role in the mitochondrial localization of human mitochondrial complex I accessory subunit NDUFB7

The present study examined human N-myristoylated proteins that specifically localize to mitochondria among the 1,705 human genes listed in MitoProteome, a mitochondrial protein database. We herein employed a strategy utilizing cellular metabolic labeling with a bioorthogonal myristic acid analog in...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports 2023-12, Vol.13 (1), p.22991-22991, Article 22991
Main Authors: Harada, Haruna, Moriya, Koko, Kobuchi, Hirotsugu, Ishihara, Naotada, Utsumi, Toshihiko
Format: Article
Language:English
Subjects:
631/337
631/45
631/80
631/92
Animals
Chlorocebus aethiops
COS Cells
Electron transport chain
Humanities and Social Sciences
Humans
Localization
Mitochondria
Mitochondria - genetics
Mitochondria - metabolism
Mitochondrial Membranes - metabolism
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
multidisciplinary
Mutants
Myristic Acid - metabolism
Myristoylation
NADH, NADPH Oxidoreductases - metabolism
NADH-ubiquinone oxidoreductase
Protein Processing, Post-Translational
Proteins
Science
Science (multidisciplinary)
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The present study examined human N-myristoylated proteins that specifically localize to mitochondria among the 1,705 human genes listed in MitoProteome, a mitochondrial protein database. We herein employed a strategy utilizing cellular metabolic labeling with a bioorthogonal myristic acid analog in transfected COS-1 cells established in our previous studies. Four proteins, DMAC1, HCCS, NDUFB7, and PLGRKT, were identified as N-myristoylated proteins that specifically localize to mitochondria. Among these proteins, DMAC1 and NDUFB7 play critical roles in the assembly of complex I of the mitochondrial respiratory chain. DMAC1 functions as an assembly factor, and NDUFB7 is an accessory subunit of complex I. An analysis of the intracellular localization of non-myristoylatable G2A mutants revealed that protein N-myristoylation occurring on NDUFB7 was important for the mitochondrial localization of this protein. Furthermore, an analysis of the role of the CHCH domain in NDUFB7 using Cys to Ser mutants revealed that it was essential for the mitochondrial localization of NDUFB7. Therefore, the present results showed that NDUFB7, a vital component of human mitochondrial complex I, was N-myristoylated, and protein N-myrisotylation and the CHCH domain were both indispensable for the specific targeting and localization of NDUFB7 to mitochondria.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-023-50390-z