Published online July 23, 2007
doi:10.1083/jcb.200702167
The Journal of Cell Biology, Vol. 178, No. 3, 399-410
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Motley et al.
Yeast peroxisomes multiply by growth and division
Alison M. Motley and
Ewald H. Hettema
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, England, UK
Correspondence to Ewald H. Hettema: e.hettema{at}sheffield.ac.uk
Peroxisomes can arise de novo from the endoplasmic reticulum (ER) via a maturation process. Peroxisomes can also multiply by fission. We have investigated how these modes of multiplication contribute to peroxisome numbers in Saccharomyces cerevisiae and the role of the dynamin-related proteins (Drps) in these processes. We have developed pulse-chase and mating assays to follow the fate of existing peroxisomes, de novo–formed peroxisomes, and ER-derived preperoxisomal structures. We find that in wild-type (WT) cells, peroxisomes multiply by fission and do not form de novo. A marker for the maturation pathway, Pex3-GFP, is delivered from the ER to existing peroxisomes. Strikingly, cells lacking peroxisomes as a result of a segregation defect do form peroxisomes de novo. This process is slower than peroxisome multiplication in WT cells and is Drp independent. In contrast, peroxisome fission is Drp dependent. Our results show that peroxisomes multiply by growth and division under our assay conditions. We conclude that the ER to peroxisome pathway functions to supply existing peroxisomes with essential membrane constituents.
Abbreviations used in this paper: Drp, dynamin-related protein; PTS1, peroxisome-targeting signal type 1; WT, wild type.

CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
Related Article
-
Splitting the difference on peroxisomes
- Mitch Leslie
J. Cell Biol. 2007 178: 338a.
[Full Text]
[PDF]
This article has been cited by other articles:
-
Hettema, E. H., Motley, A. M.
(2009). How peroxisomes multiply. J. Cell Sci.
122: 2331-2336
[Abstract]
[Full Text]
-
Perry, R. J., Mast, F. D., Rachubinski, R. A.
(2009). Endoplasmic Reticulum-Associated Secretory Proteins Sec20p, Sec39p, and Dsl1p Are Involved in Peroxisome Biogenesis. Eukaryot Cell
8: 830-843
[Abstract]
[Full Text]
-
Halbach, A., Rucktaschel, R., Rottensteiner, H., Erdmann, R.
(2009). The N-domain of Pex22p Can Functionally Replace the Pex3p N-domain in Targeting and Peroxisome Formation. J. Biol. Chem.
284: 3906-3916
[Abstract]
[Full Text]
-
Raychaudhuri, S., Prinz, W. A.
(2008). Nonvesicular phospholipid transfer between peroxisomes and the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA
105: 15785-15790
[Abstract]
[Full Text]
-
Lingard, M. J., Gidda, S. K., Bingham, S., Rothstein, S. J., Mullen, R. T., Trelease, R. N.
(2008). Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A Cooperate in Cell Cycle-Associated Replication of Peroxisomes. Plant Cell
20: 1567-1585
[Abstract]
[Full Text]
-
Motley, A. M., Ward, G. P., Hettema, E. H.
(2008). Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. J. Cell Sci.
121: 1633-1640
[Abstract]
[Full Text]
-
Yan, M., Rachubinski, D. A., Joshi, S., Rachubinski, R. A., Subramani, S.
(2008). Dysferlin Domain-containing Proteins, Pex30p and Pex31p, Localized to Two Compartments, Control the Number and Size of Oleate-induced Peroxisomes in Pichia pastoris. Mol. Biol. Cell
19: 885-898
[Abstract]
[Full Text]
-
Liu, F., Ng, S. K., Lu, Y., Low, W., Lai, J., Jedd, G.
(2008). Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting. JCB
180: 325-339
[Abstract]
[Full Text]