Restoration of peroxisome biogenesis in a peroxisome-deficient mammalian cell line by expression of either the 35 kDa or the 70 kDa peroxisomal membrane proteins

1994 ◽  
Vol 17 (3) ◽  
pp. 327-329 ◽  
Author(s):  
J. G�rtner ◽  
C. Obie ◽  
P. Watkins ◽  
D. Valle
1992 ◽  
Vol 225 (4) ◽  
pp. 331-337 ◽  
Author(s):  
Pierre Sokoloff ◽  
Marc Andrieux ◽  
Roger Besançon ◽  
Catherine Pilon ◽  
Marie-Pascale Martres ◽  
...  

1994 ◽  
Vol 3 (2) ◽  
pp. 253-256 ◽  
Author(s):  
Rosann A. Farber ◽  
Thomas D. Petes ◽  
Margaret Dominska ◽  
Sarah S. Hudgens ◽  
R.Michael Liskay

1962 ◽  
Vol 17 (4) ◽  
pp. 479 ◽  
Author(s):  
N. Delihas ◽  
M. A. Rich ◽  
M. L. Eidinoff

2011 ◽  
Vol 7 (6) ◽  
pp. e1002074 ◽  
Author(s):  
Velia Siciliano ◽  
Filippo Menolascina ◽  
Lucia Marucci ◽  
Chiara Fracassi ◽  
Immacolata Garzilli ◽  
...  

2015 ◽  
Vol 113 (1) ◽  
pp. 26-38 ◽  
Author(s):  
Amanda M. Lewis ◽  
Nicholas R. Abu-Absi ◽  
Michael C. Borys ◽  
Zheng Jian Li

2019 ◽  
Vol 13 (1) ◽  
pp. 36-42 ◽  
Author(s):  
FITHRIYAH SJATHA ◽  
◽  
OKTIVIA CHANDRA MUSTIKA ◽  
ANGKY BUDIANTI ◽  
TJAHJANI MIRAWATI SUDIRO ◽  
...  

Intervirology ◽  
1980 ◽  
Vol 13 (6) ◽  
pp. 331-341 ◽  
Author(s):  
Arthur H. Mclntosh ◽  
Rebecca Shamy

2001 ◽  
Vol 114 (11) ◽  
pp. 2199-2204 ◽  
Author(s):  
Tineke Voorn-Brouwer ◽  
Astrid Kragt ◽  
Henk F. Tabak ◽  
Ben Distel

The classic model for peroxisome biogenesis states that new peroxisomes arise by the fission of pre-existing ones and that peroxisomal matrix and membrane proteins are recruited directly from the cytosol. Recent studies challenge this model and suggest that some peroxisomal membrane proteins might traffic via the endoplasmic reticulum to peroxisomes. We have studied the trafficking in human fibroblasts of three peroxisomal membrane proteins, Pex2p, Pex3p and Pex16p, all of which have been suggested to transit the endoplasmic reticulum before arriving in peroxisomes. Here, we show that targeting of these peroxisomal membrane proteins is not affected by inhibitors of COPI and COPII that block vesicle transport in the early secretory pathway. Moreover, we have obtained no evidence for the presence of these peroxisomal membrane proteins in compartments other than peroxisomes and demonstrate that COPI and COPII inhibitors do not affect peroxisome morphology or integrity. Together, these data fail to provide any evidence for a role of the endoplasmic reticulum in peroxisome biogenesis.


1992 ◽  
Vol 12 (12) ◽  
pp. 5536-5540
Author(s):  
R J Boorstein ◽  
L N Chiu ◽  
G W Teebor

We isolated a mutant mammalian cell line lacking activity for the DNA repair enzyme 5-hydroxymethyluracil-DNA glycosylase (HmUra-DNA glycosylase). The mutant was isolated through its resistance to the thymidine analog 5-hydroxymethyl-2'-deoxyuridine (HmdUrd). The mutant incorporates HmdUrd into DNA to the same extent as the parent line but, lacking the repair enzyme, does not remove it. The phenotype of the mutant demonstrates that the toxicity of HmdUrd does not result from substitution of thymine in DNA by HmUra but rather from the removal via base excision of large numbers of HmUra residues in DNA. This finding elucidates a novel mechanism of toxicity for a xenobiotic nucleoside. Furthermore, the isolation of this line supports our hypothesis that the enzymatic repairability of HmUra derives not from its formation opposite adenine via the oxidation of thymine, but rather from its formation opposite guanine as a product of the oxidation and subsequent deamination of 5-methylcytosine.


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