Skip NavigationSkip to Content

PTIP associates with MLL3-and MLL4-containing histone H3 lysine 4 methyltransferase complex

  1. Author:
    Cho, Y. W.
    Hong, T.
    Hong, S.
    Guo, H.
    Yu, H.
    Kim, D.
    Guszczynski, T.
    Dressler, G. R.
    Copeland, T. D.
    Kalkum, M.
    Ge, K.
  2. Author Address

    NIDDK, NIH, Nucl Receptor Biol Sect, Bethesda, MD 20892 USA. City Hope Natl Med Ctr, Beckman Res Inst, Div Immunol, Duarte, CA 91010 USA. Univ Michigan, Dept Pathol, Ann Arbor, MI 48109 USA. NCI, Natl Inst Hlth, Lab Prot Dynam & Signaling, Frederick, MD 21702 USA.;Ge, K, NIDDK, NIH, Nucl Receptor Biol Sect, Bethesda, MD 20892 USA.;kaig@niddk.nih.gov
    1. Year: 2007
    2. Date: Jul
  1. Journal: Journal of Biological Chemistry
    1. 282
    2. 28
    3. Pages: 20395-20406
  2. Type of Article: Article
  3. ISSN: 0021-9258
  1. Abstract:

    PTIP, a protein with tandem BRCT domains, has been implicated in DNA damage response. However, its normal cellular functions remain unclear. Here we show that while ectopically expressed PTIP is capable of interacting with DNA damage response proteins including 53BP1, endogenous PTIP, and a novel protein PA1 are both components of a Set1-like histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, SET domain-containing HMTsMLL3 and MLL4, and substoichiometric amount of JmjC domain-containing putative histone demethylase UTX. PTIP complex carries robust HMT activity and specifically methylates lysine 4 (K4) on histone H3. Furthermore, PA1 binds PTIP directly and requires PTIP for interaction with the rest of the complex. Moreover, we show that hDPY-30 binds ASH2L directly. The evolutionarily conserved hDPY-30, ASH2L, RBBP5, and WDR5 likely constitute a subcomplex that is shared by all human Set1-likeHMTcomplexes. In contrast, PTIP, PA1, and UTX specifically associate with the PTIP complex. Thus, in cells without DNA damage agent treatment, the endogenous PTIP associates with a Set1-like HMT complex of unique subunit composition. As histone H3 K4 methylation associates with active genes, our study suggests a potential role of PTIP in the regulation of gene expression.

    See More

External Sources

  1. DOI: 10.1074/jbc.M701574200
  2. WOS: 000247819300042

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel