Abstract:
:Many newly synthesized proteins have to become unfolded during translocation across biological membranes. We have analyzed the effects of various stabilization/destabilization mutations in the Ig-like module of the muscle protein titin upon its import from the N terminus or C terminus into mitochondria. The effects of mutations on the import of the titin module from the C terminus correlate well with those on forced mechanical unfolding in atomic-force microscopy (AFM) measurements. On the other hand, as long as turnover of the mitochondrial Hsp70 system is not rate-limiting for the import, import of the titin module from the N terminus is sensitive to mutations in the N-terminal region but not the ones in the C-terminal region that affect resistance to global unfolding in AFM experiments. We propose that the mitochondrial-import system can catalyze precursor-unfolding by reducing the stability of unfolding intermediates.
journal_name
Proc Natl Acad Sci U S Aauthors
Sato T,Esaki M,Fernandez JM,Endo Tdoi
10.1073/pnas.0504495102keywords:
subject
Has Abstractpub_date
2005-12-13 00:00:00pages
17999-8004issue
50eissn
0027-8424issn
1091-6490pii
0504495102journal_volume
102pub_type
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