TY - JOUR
T1 - Myristoyl group-aided protein import into the mitochondrial intermembrane space
AU - Ueda, Eri
AU - Tamura, Yasushi
AU - Sakaue, Haruka
AU - Kawano, Shin
AU - Kakuta, Chika
AU - Matsumoto, Shunsuke
AU - Endo, Toshiya
N1 - Funding Information:
We thank members of the Endo laboratory for discussions and comments and Dr. N. Ishihara (Osaka University) for encouragement to E.U. We thank Dr. Elizabeth A. Craig for the ssc1-3 strains and Dr. Janet M. Shaw for the tom70Δtom71Δ strain. We acknowledge support of this work by JSPS KAKENHI Grant Numbers 15H05705 (T.E.), 22227003 (T.E.), 24121713 (T.E.), 19058005 (T.E.), and 17H06414 (Y.T.), a JST CREST Grant Number JPMJCR12M (T.E.), an AMED-Prime Grant Number JP18gm5910026 (Y.T.), and a grant from the Takeda Science Foundation (T.E.).
Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - The MICOS complex mediates formation of the crista junctions in mitochondria. Here we analyzed the mitochondrial import pathways for the six yeast MICOS subunits as a step toward understanding of the assembly mechanisms of the MICOS complex. Mic10, Mic12, Mic26, Mic27, and Mic60 used the presequence pathway to reach the intermembrane space (IMS). In contrast, Mic19 took the TIM40/MIA pathway, through its CHCH domain, to reach the IMS. Unlike canonical TIM40/MIA substrates, presence of the N-terminal unfolded DUF domain impaired the import efficiency of Mic19, yet N-terminal myristoylation of Mic19 circumvented this effect. The myristoyl group of Mic19 binds to Tom20 of the TOM complex as well as the outer membrane, which may lead to “entropy pushing” of the DUF domain followed by the CHCH domain of Mic19 into the import channel, thereby achieving efficient import.
AB - The MICOS complex mediates formation of the crista junctions in mitochondria. Here we analyzed the mitochondrial import pathways for the six yeast MICOS subunits as a step toward understanding of the assembly mechanisms of the MICOS complex. Mic10, Mic12, Mic26, Mic27, and Mic60 used the presequence pathway to reach the intermembrane space (IMS). In contrast, Mic19 took the TIM40/MIA pathway, through its CHCH domain, to reach the IMS. Unlike canonical TIM40/MIA substrates, presence of the N-terminal unfolded DUF domain impaired the import efficiency of Mic19, yet N-terminal myristoylation of Mic19 circumvented this effect. The myristoyl group of Mic19 binds to Tom20 of the TOM complex as well as the outer membrane, which may lead to “entropy pushing” of the DUF domain followed by the CHCH domain of Mic19 into the import channel, thereby achieving efficient import.
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U2 - 10.1038/s41598-018-38016-1
DO - 10.1038/s41598-018-38016-1
M3 - Article
C2 - 30718713
AN - SCOPUS:85061051529
SN - 2045-2322
VL - 9
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 1185
ER -