English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  ROMO1 is a constituent of the human presequence translocase required for YME1L protease import.

Richter, F., Dennerlein, S., Nikolov, M., Jans, D. C., Naumenko, N., Aich, A., et al. (2019). ROMO1 is a constituent of the human presequence translocase required for YME1L protease import. The Journal of Cell Biology, 218(2): 598. doi:10.1083/jcb.201806093.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0002-B841-5 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-F3D2-E
Genre: Journal Article

Files

show Files
hide Files
:
3016879.pdf (Publisher version), 3MB
Name:
3016879.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Richter, F., Author
Dennerlein, S., Author
Nikolov, M.1, Author              
Jans, D. C.2, Author              
Naumenko, N., Author
Aich, A., Author
MacVicar, T., Author
Linden, A.1, Author              
Jakobs, S.2, Author              
Urlaub, H.1, Author              
Langer, T., Author
Rehling, P.3, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
2Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              
3Max Planck Fellow Peter Rehling, ou_1298545              

Content

show
hide
Free keywords: -
 Abstract: The mitochondrial presequence translocation machinery (TIM23 complex) is conserved between the yeast Saccharomyces cerevisiae and humans; however, functional characterization has been mainly performed in yeast. Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life. Analyses of a ROMO1 knockout cell line revealed aberrant inner membrane structure and altered processing of the GTPase OPA1. We show that in the absence of ROMO1, mitochondria lose the inner membrane YME1L protease, which participates in OPA1 processing and ROMO1 turnover. While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L. This selective import defect can be linked to charge distribution in the unusually long targeting sequence of YME1L. Our analyses establish an unexpected link between mitochondrial protein import and inner membrane protein quality control.

Details

show
hide
Language(s): eng - English
 Dates: 2018-12-312019-02-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1083/jcb.201806093
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Cell Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 17 Volume / Issue: 218 (2) Sequence Number: 598 Start / End Page: - Identifier: -