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Machinery for protein sorting and assembly in the mitochondrial outer membrane
The results suggest that the TOM complex, which can transport all kinds of mitochondrial precursor proteins, is not sufficient for the correct integration of outer membrane proteins with a complicated topology, and instead transfers precursor proteins to the SAM complex.
The Yeast Nα-Acetyltransferase NatA Is Quantitatively Anchored to the Ribosome and Interacts with Nascent Polypeptides
- M. Gautschi, S. Just, +5 authors S. Rospert
- Medicine, BiologyMolecular and Cellular Biology
- 15 October 2003
The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis.
Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis.
- Karina von der Malsburg, Judith M. Müller, +21 authors M. van der Laan
- Medicine, BiologyDevelopmental cell
- 18 October 2011
The findings indicate that mitofilin is a central component of MINOS and functions as a multifunctional regulator of mitochondrial architecture and protein biogenesis.
RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin
- M. Gautschi, H. Lilie, +5 authors S. Rospert
- Biology, MedicineProceedings of the National Academy of Sciences…
- 27 March 2001
This work has identified the DnaK homolog Ssz1p/Pdr13p as zuotin's partner chaperone, and confirmed the existence of a functional complex RAC, which stimulates the translocation of a ribosome-bound mitochondrial precursor protein into mitochondria, providing evidence for its chaper one-like effect on nascent chains.
A functional chaperone triad on the yeast ribosome
- M. Gautschi, A. Mun, S. Ross, S. Rospert
- Medicine, BiologyProceedings of the National Academy of Sciences…
- 2 April 2002
In vitro and in vivo data supports a model in which Ssb1/2p, Ssz1p, and zuotin act in concert on nascent chains while they are being synthesized, and an efficient crosslink of the nascent chain to Ssb2p depends on the presence of functional RAC.
The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
- P. Huang, M. Gautschi, W. Walter, S. Rospert, E. Craig
- Biology, MedicineNature Structural &Molecular Biology
- 22 May 2005
It is proposed that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone.
Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the ‘acid chain’ hypothesis
- T. Komiya, S. Rospert, C. Koehler, R. Looser, G. Schatz, K. Mihara
- Biology, MedicineThe EMBO journal
- 15 July 1998
The apparent affinity and salt resistance of precursor binding increased in the order Tom20, and the interaction of mitochondrial precursors with three acidic receptor domains was assayed.
Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria.
- Dusanka Milenkovic, Thomas M. Ramming, +6 authors A. Chacińska
- Biology, MedicineMolecular biology of the cell
- 15 May 2009
This study found that a region within the Tim9 and Tim10 precursors functions as a signal for the engagement of substrate proteins with the Mia40 receptor, and contains sufficient information to facilitate the transfer of proteins across the outer membrane to the intermembrane space.
Sequential action of two hsp70 complexes during protein import into mitochondria
- M. Horst, W. Oppliger, S. Rospert, H. Schönfeld, G. Schatz, A. Azem
- Biology, MedicineThe EMBO journal
- 15 April 1997
The mitochondrial chaperone mhsp70 mediates protein transport across the inner membrane and protein folding in the matrix and can function as part of two different complexes within the same organelle.
Transcriptional activation of polycomb-repressed genes by ZRF1
It is shown in human cell lines that ZRF1 (zuotin-related factor 1) is specifically recruited to histone H2A when it is ubiquitinated at Lys 119 by means of a novel ubiquitin-interacting domain that is located in the evolutionarily conserved zuotin domain.