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Hpz1 Modulates the G1-S Transition in Fission Yeast

Here we characterize a novel protein in S. pombe. It has a high degree of homology with the Zn-finger domain of the human Poly(ADP-ribose) polymerase (PARP). Surprisingly, the gene for this protein is, in many fungi, fused with and in the same reading frame as that encoding Rad3, the homologue of th...

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Autores principales: Bøe, Cathrine A., Knutsen, Jon Halvor J., Boye, Erik, Grallert, Beáta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3435320/
https://www.ncbi.nlm.nih.gov/pubmed/22970243
http://dx.doi.org/10.1371/journal.pone.0044539
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author Bøe, Cathrine A.
Knutsen, Jon Halvor J.
Boye, Erik
Grallert, Beáta
author_facet Bøe, Cathrine A.
Knutsen, Jon Halvor J.
Boye, Erik
Grallert, Beáta
author_sort Bøe, Cathrine A.
collection PubMed
description Here we characterize a novel protein in S. pombe. It has a high degree of homology with the Zn-finger domain of the human Poly(ADP-ribose) polymerase (PARP). Surprisingly, the gene for this protein is, in many fungi, fused with and in the same reading frame as that encoding Rad3, the homologue of the human ATR checkpoint protein. We name the protein Hpz1 (Homologue of PARP-type Zn-finger). Hpz1 does not possess PARP activity, but is important for resistance to ultraviolet light in the G1 phase and to treatment with hydroxyurea, a drug that arrests DNA replication forks in the S phase. However, we find no evidence of a checkpoint function of Hpz1. Furthermore, absence of Hpz1 results in an advancement of S-phase entry after a G1 arrest as well as earlier recovery from a hydroxyurea block. The hpz1 gene is expressed mainly in the G1 phase and Hpz1 is localized to the nucleus. We conclude that Hpz1 regulates the initiation of the S phase and may cooperate with Rad3 in this function.
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spelling pubmed-34353202012-09-11 Hpz1 Modulates the G1-S Transition in Fission Yeast Bøe, Cathrine A. Knutsen, Jon Halvor J. Boye, Erik Grallert, Beáta PLoS One Research Article Here we characterize a novel protein in S. pombe. It has a high degree of homology with the Zn-finger domain of the human Poly(ADP-ribose) polymerase (PARP). Surprisingly, the gene for this protein is, in many fungi, fused with and in the same reading frame as that encoding Rad3, the homologue of the human ATR checkpoint protein. We name the protein Hpz1 (Homologue of PARP-type Zn-finger). Hpz1 does not possess PARP activity, but is important for resistance to ultraviolet light in the G1 phase and to treatment with hydroxyurea, a drug that arrests DNA replication forks in the S phase. However, we find no evidence of a checkpoint function of Hpz1. Furthermore, absence of Hpz1 results in an advancement of S-phase entry after a G1 arrest as well as earlier recovery from a hydroxyurea block. The hpz1 gene is expressed mainly in the G1 phase and Hpz1 is localized to the nucleus. We conclude that Hpz1 regulates the initiation of the S phase and may cooperate with Rad3 in this function. Public Library of Science 2012-09-06 /pmc/articles/PMC3435320/ /pubmed/22970243 http://dx.doi.org/10.1371/journal.pone.0044539 Text en © 2012 Bøe et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Bøe, Cathrine A.
Knutsen, Jon Halvor J.
Boye, Erik
Grallert, Beáta
Hpz1 Modulates the G1-S Transition in Fission Yeast
title Hpz1 Modulates the G1-S Transition in Fission Yeast
title_full Hpz1 Modulates the G1-S Transition in Fission Yeast
title_fullStr Hpz1 Modulates the G1-S Transition in Fission Yeast
title_full_unstemmed Hpz1 Modulates the G1-S Transition in Fission Yeast
title_short Hpz1 Modulates the G1-S Transition in Fission Yeast
title_sort hpz1 modulates the g1-s transition in fission yeast
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3435320/
https://www.ncbi.nlm.nih.gov/pubmed/22970243
http://dx.doi.org/10.1371/journal.pone.0044539
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