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Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
Nagotu, S., Saraya, R., Otzen, M., Veenhuis, M. & van der Klei, I. J., May-2008, In : Biochimica et Biophysica Acta-Molecular Cell Research. 1783, 5, p. 760-769 10 p.Research output: Contribution to journal › Article › Academic › peer-review
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Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation. / Nagotu, Shinisha; Saraya, Ruchi; Otzen, Marleen; Veenhuis, Marten; van der Klei, Ida J.
In: Biochimica et Biophysica Acta-Molecular Cell Research, Vol. 1783, No. 5, 05.2008, p. 760-769.Research output: Contribution to journal › Article › Academic › peer-review
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TY - JOUR
T1 - Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
AU - Nagotu, Shinisha
AU - Saraya, Ruchi
AU - Otzen, Marleen
AU - Veenhuis, Marten
AU - van der Klei, Ida J.
PY - 2008/5
Y1 - 2008/5
N2 - We show that the dynamin-like proteins Dnm1p and Vps1p are not required for re-introduction of peroxisomes in Hansenula polymorpha pex3 cells upon complementation with PEX3-GFP. Instead, Dnm1p, but not Vps1p, plays a crucial role in organelle proliferation via fission. In H. polymorpha DNM1 deletion cells (dnm1) a single peroxisome is present that forms long extensions, which protrude into developing buds and divide during cytokinesis. Budding pex11.dnm1 double deletion cells lack these peroxisomal extensions, suggesting that the peroxisomal membrane protein Pex11p is required for their formation. Life cell imaging revealed that fluorescent Dnm1p-GFP spots fluctuate between peroxisomes and mitochondria. On the other hand Pex11p is present over the entire organelle surface, but concentrates during fission at the basis of the organelle extension in dnm1 cells. Our data indicate that peroxisome fission is the major pathway for peroxisome multiplication in H. polymorpha. (C) 2007 Elsevier B.V. All rights reserved.
AB - We show that the dynamin-like proteins Dnm1p and Vps1p are not required for re-introduction of peroxisomes in Hansenula polymorpha pex3 cells upon complementation with PEX3-GFP. Instead, Dnm1p, but not Vps1p, plays a crucial role in organelle proliferation via fission. In H. polymorpha DNM1 deletion cells (dnm1) a single peroxisome is present that forms long extensions, which protrude into developing buds and divide during cytokinesis. Budding pex11.dnm1 double deletion cells lack these peroxisomal extensions, suggesting that the peroxisomal membrane protein Pex11p is required for their formation. Life cell imaging revealed that fluorescent Dnm1p-GFP spots fluctuate between peroxisomes and mitochondria. On the other hand Pex11p is present over the entire organelle surface, but concentrates during fission at the basis of the organelle extension in dnm1 cells. Our data indicate that peroxisome fission is the major pathway for peroxisome multiplication in H. polymorpha. (C) 2007 Elsevier B.V. All rights reserved.
KW - peroxisome
KW - yeast
KW - dynamin-like protein
KW - Dnm1p
KW - Pex11p
KW - DYNAMIN-RELATED GTPASE
KW - SACCHAROMYCES-CEREVISIAE
KW - MITOCHONDRIAL FISSION
KW - ENDOPLASMIC-RETICULUM
KW - PROTEIN
KW - DIVISION
KW - YEAST
KW - MEMBRANE
KW - PEX3P
KW - BIOGENESIS
U2 - 10.1016/j.bbamcr.2007.10.018
DO - 10.1016/j.bbamcr.2007.10.018
M3 - Article
VL - 1783
SP - 760
EP - 769
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
SN - 0167-4889
IS - 5
ER -
ID: 4722629