Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2003 Nov 24;163(4):707–713. doi: 10.1083/jcb.200308004

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2003, The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 4. — The J-domain stimulates the ATPase activity of mtHsp70 and influences the Tim44–mtHsp70 interaction. (A) ATPase activity of mtHsp70 under steady-state conditions using [α³²P]ATP, purified mtHsp70, Mge1, and the J-domain of the 18-kD protein of PAM. Purified Tim44 did not stimulate the ATPase activity. (B) Disturbance of the Tim44–mtHsp70 interaction in J mutant (ts) mitochondria. Mitochondria were lysed under nondenaturing conditions and subjected to coprecipitation with antibodies directed against Tim44 or mtHsp70 (Voisine et al., 1999). Precipitates were analyzed by SDS-PAGE and immunodecoration (5% of the mitochondrial extracts are shown). Quantification: the amount of coprecipitated protein from wild type under ATP-depleted conditions was set to 100% (control). (C) Blue native PAGE of mitochondria lysed with digitonin, followed by immunodecoration with antibodies directed against Tim23, Tim22, and Tom40. (D) Protein A tagged Tim23 was expressed in wild-type and J mutant cells. Mitochondria were isolated, lysed with digitonin, and subjected to IgG chromatography.