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Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation

Here, we describe a novel peroxin, Pex37, in the yeast Hansenula polymorpha. H. polymorpha Pex37 is a peroxisomal membrane protein, which belongs to a protein family that includes, among others, the Neurospora crassa Woronin body protein Wsc, the human peroxisomal membrane protein PXMP2, the Sacchar...

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Autores principales: Singh, Ritika, Manivannan, Selvambigai, Krikken, Arjen M., de Boer, Rinse, Bordin, Nicola, Devos, Damien P., van der Klei, Ida J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7318627/
https://www.ncbi.nlm.nih.gov/pubmed/31692262
http://dx.doi.org/10.1111/febs.15123
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author Singh, Ritika
Manivannan, Selvambigai
Krikken, Arjen M.
de Boer, Rinse
Bordin, Nicola
Devos, Damien P.
van der Klei, Ida J.
author_facet Singh, Ritika
Manivannan, Selvambigai
Krikken, Arjen M.
de Boer, Rinse
Bordin, Nicola
Devos, Damien P.
van der Klei, Ida J.
author_sort Singh, Ritika
collection PubMed
description Here, we describe a novel peroxin, Pex37, in the yeast Hansenula polymorpha. H. polymorpha Pex37 is a peroxisomal membrane protein, which belongs to a protein family that includes, among others, the Neurospora crassa Woronin body protein Wsc, the human peroxisomal membrane protein PXMP2, the Saccharomyces cerevisiae mitochondrial inner membrane protein Sym1, and its mammalian homologue MPV17. We show that deletion of H. polymorpha PEX37 does not appear to have a significant effect on peroxisome biogenesis or proliferation in cells grown at peroxisome‐inducing growth conditions (methanol). However, the absence of Pex37 results in a reduction in peroxisome numbers and a defect in peroxisome segregation in cells grown at peroxisome‐repressing conditions (glucose). Conversely, overproduction of Pex37 in glucose‐grown cells results in an increase in peroxisome numbers in conjunction with a decrease in their size. The increase in numbers in PEX37‐overexpressing cells depends on the dynamin‐related protein Dnm1. Together our data suggest that Pex37 is involved in peroxisome fission in glucose‐grown cells. Introduction of human PXMP2 in H. polymorpha pex37 cells partially restored the peroxisomal phenotype, indicating that PXMP2 represents a functional homologue of Pex37. H.polymorpha pex37 cells did not show aberrant growth on any of the tested carbon and nitrogen sources that are metabolized by peroxisomal enzymes, suggesting that Pex37 may not fulfill an essential function in transport of these substrates or compounds required for their metabolism across the peroxisomal membrane.
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spelling pubmed-73186272020-06-29 Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation Singh, Ritika Manivannan, Selvambigai Krikken, Arjen M. de Boer, Rinse Bordin, Nicola Devos, Damien P. van der Klei, Ida J. FEBS J Editor's Choice Here, we describe a novel peroxin, Pex37, in the yeast Hansenula polymorpha. H. polymorpha Pex37 is a peroxisomal membrane protein, which belongs to a protein family that includes, among others, the Neurospora crassa Woronin body protein Wsc, the human peroxisomal membrane protein PXMP2, the Saccharomyces cerevisiae mitochondrial inner membrane protein Sym1, and its mammalian homologue MPV17. We show that deletion of H. polymorpha PEX37 does not appear to have a significant effect on peroxisome biogenesis or proliferation in cells grown at peroxisome‐inducing growth conditions (methanol). However, the absence of Pex37 results in a reduction in peroxisome numbers and a defect in peroxisome segregation in cells grown at peroxisome‐repressing conditions (glucose). Conversely, overproduction of Pex37 in glucose‐grown cells results in an increase in peroxisome numbers in conjunction with a decrease in their size. The increase in numbers in PEX37‐overexpressing cells depends on the dynamin‐related protein Dnm1. Together our data suggest that Pex37 is involved in peroxisome fission in glucose‐grown cells. Introduction of human PXMP2 in H. polymorpha pex37 cells partially restored the peroxisomal phenotype, indicating that PXMP2 represents a functional homologue of Pex37. H.polymorpha pex37 cells did not show aberrant growth on any of the tested carbon and nitrogen sources that are metabolized by peroxisomal enzymes, suggesting that Pex37 may not fulfill an essential function in transport of these substrates or compounds required for their metabolism across the peroxisomal membrane. John Wiley and Sons Inc. 2019-11-26 2020-05 /pmc/articles/PMC7318627/ /pubmed/31692262 http://dx.doi.org/10.1111/febs.15123 Text en © 2019 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Editor's Choice
Singh, Ritika
Manivannan, Selvambigai
Krikken, Arjen M.
de Boer, Rinse
Bordin, Nicola
Devos, Damien P.
van der Klei, Ida J.
Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title_full Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title_fullStr Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title_full_unstemmed Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title_short Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation
title_sort hansenula polymorpha pex37 is a peroxisomal membrane protein required for organelle fission and segregation
topic Editor's Choice
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7318627/
https://www.ncbi.nlm.nih.gov/pubmed/31692262
http://dx.doi.org/10.1111/febs.15123
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