TY  - JOUR
A1  - Singh, Jasbir
A1  - Singh, S.
A1  - Dani, H. M.
A1  - Sharma, Reeta
A1  - Steinberg, Pablo
T1  - Interactions of aflatoxin B-1 with SRP components can disrupt protein targeting
N2  - Spectrofluorimetric studies have revealed that aflatoxin B-1 (AFB(1)) interacts with signal recognition particle (SRP), which acts as an escort for polyribosomes with signal peptides to be transported and bound to the cytoplasmic face of the endoplasmic reticulum (ER). We further report that the binding of AFB(1) to SRP is selective as it only binds to two (SRP9 and 14) out of its three constituent polypeptides studied. Binding of AFB(1) to proteins is known to alter their conformations. Interactions of AFB(1) with SRP polypeptides may generate structural and functional alterations in this particle and hinder secretory protein synthesis. Copyright (C) 2004 John Wiley Sons, Ltd
Y1  - 2005
SN  - 0263-6484
ER  - 
TY  - JOUR
A1  - Thierbach, Renè
A1  - Schulz, Tim Julius
A1  - Isken, Frank
A1  - Voigt, Aanja
A1  - Mietzner, Brun
A1  - Drewes, Gunnar
A1  - von Kleist-Retzow, Jürgen-Christoph
A1  - Wiesner, Rudolf J.
A1  - Magnuson, Mark A.
A1  - Puccio, Helene
A1  - Pfeiffer, Andreas F. H.
A1  - Steinberg, Pablo
A1  - Ristow, Michael
T1  - Targeted disruption of hepatic frataxin expression causes impaired mitochondrial function, decreased life span and tumor growth in mice
N2  - We have disrupted expression of the mitochondrial Friedreich ataxia protein frataxin specifically in murine hepatocytes to generate mice with impaired mitochondrial function and decreased oxidative phosphorylation. These animals have a reduced life span and develop multiple hepatic tumors. Livers also show increased oxidative stress, impaired respiration and reduced ATP levels paralleled by reduced activity of iron-sulfur cluster (Fe/S) containing proteins (ISP), which all leads to increased hepatocyte turnover by promoting both apoptosis and proliferation. Accordingly, phosphorylation of the stress-inducible p38 MAP kinase was found to be specifically impaired following disruption of frataxin. Taken together, these findings indicate that frataxin may act as a mitochondrial tumor suppressor protein in mammals
Y1  - 2005
ER  -