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  1. Article: The Fission Yeast Inhibitor of Growth (ING) Protein Png1p Functions in Response to DNA Damage

    Chen, Jian-Qiang / Li, Yang / Pan, Xian / Lei, Bing-Kun / Chang, Cheng / Liu, Zheng-Xun / Lu, Hong

    Journal of biological chemistry. 2010 May 21, v. 285, no. 21

    2010  

    Abstract: In budding yeast and human cells, ING (inhibitor of growth) tumor suppressor proteins play important roles in response to DNA damage by modulating chromatin structure through collaborating with histone acetyltransferase or histone deacetylase complexes. ... ...

    Abstract In budding yeast and human cells, ING (inhibitor of growth) tumor suppressor proteins play important roles in response to DNA damage by modulating chromatin structure through collaborating with histone acetyltransferase or histone deacetylase complexes. However, the biological functions of ING family proteins in fission yeast are poorly defined. Here, we report that Png1p, a fission yeast ING homolog protein, is required for cell growth under normal and DNA-damaged conditions. Png1p was further confirmed to regulate histone H4 acetylation through collaboration with the MYST family histone acetyltransferase 1 (Mst1). Additionally, both fission yeast PNG1 and MST1 can functionally complement their budding yeast correspondence homologs YNG2 and ESA1, respectively. These results suggest that ING proteins in fission yeast might also conserve function, similar to ING proteins in budding yeast and human cells. We also showed that decreased acetylation in Δpng1 cells resulted in genome-wide down-regulation of 756 open reading frames, including the central DNA repair gene RAD22. Overexpression of RAD22 partially rescued the png1 mutant phenotype under both normal and DNA-damaged conditions. Furthermore, decreased expression of RAD22 in Δpng1 cells was confirmed to be caused by decreased H4 acetylation at its promoter. Altogether, these results indicate that Png1p is required for histone H4 acetylation and functions upstream of RAD22 in the DNA damage response pathway.
    Language English
    Dates of publication 2010-0521
    Size p. 15786-15793.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: The fission yeast inhibitor of growth (ING) protein Png1p functions in response to DNA damage.

    Chen, Jian-Qiang / Li, Yang / Pan, Xian / Lei, Bing-Kun / Chang, Cheng / Liu, Zheng-Xun / Lu, Hong

    The Journal of biological chemistry

    2010  Volume 285, Issue 21, Page(s) 15786–15793

    Abstract: In budding yeast and human cells, ING (inhibitor of growth) tumor suppressor proteins play important roles in response to DNA damage by modulating chromatin structure through collaborating with histone acetyltransferase or histone deacetylase complexes. ... ...

    Abstract In budding yeast and human cells, ING (inhibitor of growth) tumor suppressor proteins play important roles in response to DNA damage by modulating chromatin structure through collaborating with histone acetyltransferase or histone deacetylase complexes. However, the biological functions of ING family proteins in fission yeast are poorly defined. Here, we report that Png1p, a fission yeast ING homolog protein, is required for cell growth under normal and DNA-damaged conditions. Png1p was further confirmed to regulate histone H4 acetylation through collaboration with the MYST family histone acetyltransferase 1 (Mst1). Additionally, both fission yeast PNG1 and MST1 can functionally complement their budding yeast correspondence homologs YNG2 and ESA1, respectively. These results suggest that ING proteins in fission yeast might also conserve function, similar to ING proteins in budding yeast and human cells. We also showed that decreased acetylation in Deltapng1 cells resulted in genome-wide down-regulation of 756 open reading frames, including the central DNA repair gene RAD22. Overexpression of RAD22 partially rescued the png1 mutant phenotype under both normal and DNA-damaged conditions. Furthermore, decreased expression of RAD22 in Deltapng1 cells was confirmed to be caused by decreased H4 acetylation at its promoter. Altogether, these results indicate that Png1p is required for histone H4 acetylation and functions upstream of RAD22 in the DNA damage response pathway.
    MeSH term(s) Acetylation ; Chromatin/genetics ; Chromatin/metabolism ; DNA Damage/physiology ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal/physiology ; Histone Acetyltransferases/genetics ; Histone Acetyltransferases/metabolism ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Histones/genetics ; Histones/metabolism ; Humans ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism
    Chemical Substances Chromatin ; DNA-Binding Proteins ; Histones ; Png1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Tumor Suppressor Proteins ; rad52 protein, S pombe ; Histone Acetyltransferases (EC 2.3.1.48) ; Histone Deacetylases (EC 3.5.1.98)
    Language English
    Publishing date 2010-03-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M110.101832
    Database MEDical Literature Analysis and Retrieval System OnLINE

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