TY  - JOUR
A1  - Zaikin, Alexey
A1  - Kurths, Jürgen
T1  - Optimal length transportation hypothesis to model proteasome product size distribution
JF  - Journal of biological physics : emphasizing physical principles in biological research ; an international journal for the formulation and application of mathematical models in the biological sciences
N2  - This paper discusses translocation features of the 20S proteasome in order to explain typical proteasome length distributions. We assume that the protein transport depends significantly on the fragment length with some optimal length which is transported most efficiently. By means of a simple one-channel model, we show that this hypothesis can explain both the one- and the three-peak length distributions found in experiments. A possible mechanism of such translocation is provided by so-called fluctuation-driven transport.
KW  - proteasome
KW  - protein translocation
KW  - stochastic process
KW  - ratchets
Y1  - 2006
U6  - https://doi.org/10.1007/s10867-006-9014-z
SN  - 0092-0606
VL  - 32
IS  - 3-4
SP  - 231
EP  - 243
PB  - Springer
CY  - Dordrecht
ER  - 
TY  - JOUR
A1  - Singh, Jasbir
A1  - Dani, Harinder M.
A1  - Sharma, Reeta
A1  - Steinberg, Pablo
T1  - Inhibition of the biosynthesis of SRP polypeptides and secretory proteins by aflatoxin B-1 can disrupt protein targeting
JF  - Cell biochemistry and function
N2  - Cell culture and western blotting studies revealed that aflatoxin B-1 (AFB(1)) inhibits the biosynthesis of two of the constituent polypeptides of signal recognition particle (SRP) (SRP54 and 72). SRP escorts polyribosomes carrying signal peptides from free form in the cytosol to the bound form on endoplasmic reticulum (ER) membrane during protein targeting. These effects of AFB(1) on SRP biosynthesis may inhibit the formation of functional SRP Our experiments have further shown that AFB(1) also inhibits the biosynthesis/translocation of a secretory protein, preprolactin, which fails to appear in the lumen of ER consequent to the treatment with this hepatocarcinogen. The results of the experiments presented in this article therefore enable us to infer for the first time that aflatoxin B-1 may inhibit the functioning of SRP as an escort and deplete the ER of polyribosomes for secretory protein synthesis. As these secretory proteins are important components of the plasma membrane, gap junctions and intercellular matrix, their absence from these locations could disturb cell to cell communication leading to tumorigenesis.
KW  - aflatoxin B-1
KW  - SRP
KW  - protein targeting
KW  - protein translocation
KW  - western blotting
Y1  - 2005
U6  - https://doi.org/10.1027/cbf.1285
SN  - 0263-6484
VL  - 24
SP  - 507
EP  - 510
PB  - Wiley
CY  - Chichester
ER  -