Role of the membrane potential in mitochondrial protein unfolding and import.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
21 05 2019
21 05 2019
Historique:
received:
16
02
2016
accepted:
10
05
2019
entrez:
23
5
2019
pubmed:
23
5
2019
medline:
21
10
2020
Statut:
epublish
Résumé
Newly synthesized mitochondrial precursor proteins have to become unfolded to cross the mitochondrial membranes. This unfolding is achieved primarily by mitochondrial Hsp70 (mtHsp70) for presequence-containing precursor proteins. However, the membrane potential across the inner membrane (ΔΨ) could also contribute to unfolding of short-presequence containing mitochondrial precursor proteins. Here we investigated the role of ΔΨ in mitochondrial protein unfolding and import. We found that the effects of mutations in the presequence on import rates are correlated well with the hydrophobicity or ability to interact with import motor components including mtHsp70, but not with ΔΨ (negative inside). A spontaneously unfolded precursor protein with a short presequence is therefore trapped by motor components including mtHsp70, but not ΔΨ, which could cause global unfolding of the precursor protein. Instead, ΔΨ may contribute the precursor unfolding by holding the presequence at the inner membrane for trapping of the unfolded species by the import motor system.
Identifiants
pubmed: 31114030
doi: 10.1038/s41598-019-44152-z
pii: 10.1038/s41598-019-44152-z
pmc: PMC6529458
doi:
Substances chimiques
Mitochondrial Proteins
0
Protein Precursors
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7637Références
Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):17999-8004
pubmed: 16326810
EMBO J. 1998 Nov 16;17(22):6497-507
pubmed: 9822595
Biol Chem. 2009 Aug;390(8):723-30
pubmed: 19453276
J Biol Chem. 2008 Oct 3;283(40):27325-32
pubmed: 18678864
J Biol Chem. 1991 Sep 25;266(27):18051-7
pubmed: 1833391
Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11770-5
pubmed: 10518525
Cell. 1993 Nov 19;75(4):717-28
pubmed: 7902213
Nat Struct Biol. 1999 Dec;6(12):1132-8
pubmed: 10581555
Structure. 2001 Jul 3;9(7):615-25
pubmed: 11470436
EMBO Rep. 2014 Jun;15(6):678-85
pubmed: 24781695
EMBO J. 1997 Apr 1;16(7):1501-7
pubmed: 9130695
Nat Struct Biol. 2002 Apr;9(4):301-7
pubmed: 11887183
Annu Rev Biochem. 2007;76:723-49
pubmed: 17263664
Nature. 1991 Oct 24;353(6346):726-30
pubmed: 1834945
Cell. 1999 May 28;97(5):565-74
pubmed: 10367886
Science. 1994 Nov 18;266(5188):1250-3
pubmed: 7973708
Cell. 2009 Oct 16;139(2):428-39
pubmed: 19837041
Trends Biochem Sci. 2004 Nov;29(11):593-600
pubmed: 15501678
Nat Rev Mol Cell Biol. 2002 Aug;3(8):555-65
pubmed: 12154367
FEBS Lett. 1990 Nov 26;275(1-2):190-4
pubmed: 2148157
EMBO J. 2002 Jul 15;21(14):3659-71
pubmed: 12110579
J Mol Biol. 1994 Jan 21;235(3):848-54
pubmed: 8289323
EMBO Rep. 2014 Jun;15(6):670-7
pubmed: 24781694
Cell. 1996 Oct 4;87(1):33-41
pubmed: 8858146
Cell. 2009 Aug 21;138(4):628-44
pubmed: 19703392
Science. 2003 Apr 4;300(5616):139-41
pubmed: 12677068
EMBO J. 1999 Jul 1;18(13):3667-75
pubmed: 10393182
EMBO J. 1997 Nov 17;16(22):6727-36
pubmed: 9362487
Cell. 2002 Nov 15;111(4):519-28
pubmed: 12437925
J Biol Chem. 2008 Feb 15;283(7):3799-807
pubmed: 18063580
Biophys J. 2004 Jun;86(6):3647-52
pubmed: 15189861
Proc Natl Acad Sci U S A. 1997 Jan 21;94(2):485-90
pubmed: 9012810
J Biol Chem. 1995 Jun 16;270(24):14267-9
pubmed: 7782281
J Cell Biol. 1993 Oct;123(1):109-17
pubmed: 8408191
Nat Rev Microbiol. 2016 Jan;14(1):33-44
pubmed: 26639779
Cell. 1995 Jan 13;80(1):11-4
pubmed: 7813006