Biochemical characterisation of the SWI/SNF family member HLTF

Craig MacKay, Rachel Toth, John Rouse

    Research output: Contribution to journalArticle

    25 Citations (Scopus)

    Abstract

    HLTF is highly similar in domain organisation to yeast Rad5. We identify PTIP and RPA70, both involved in DNA replication and DNA repair, as HLTF-interacting proteins although cells depleted of HLTF did not show defects in cellular responses to DNA damage. In vitro, HLTF has ATPase activity and E3 ubiquitin ligase activity with a range of E2 ubiquitin conjugating enzymes. HLTF expression is severely reduced in a range of cancer cells, and we suggest that the HLTF antibodies generated in this study could be used for cancer diagnostic purposes. (C) 2009 Elsevier Inc. All rights reserved.

    Original languageEnglish
    Pages (from-to)187-191
    Number of pages5
    JournalBiochemical and Biophysical Research Communications
    Volume390
    Issue number2
    DOIs
    Publication statusPublished - 11 Dec 2009

    Cite this

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    abstract = "HLTF is highly similar in domain organisation to yeast Rad5. We identify PTIP and RPA70, both involved in DNA replication and DNA repair, as HLTF-interacting proteins although cells depleted of HLTF did not show defects in cellular responses to DNA damage. In vitro, HLTF has ATPase activity and E3 ubiquitin ligase activity with a range of E2 ubiquitin conjugating enzymes. HLTF expression is severely reduced in a range of cancer cells, and we suggest that the HLTF antibodies generated in this study could be used for cancer diagnostic purposes. (C) 2009 Elsevier Inc. All rights reserved.",
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    Biochemical characterisation of the SWI/SNF family member HLTF. / MacKay, Craig; Toth, Rachel; Rouse, John.

    In: Biochemical and Biophysical Research Communications, Vol. 390, No. 2, 11.12.2009, p. 187-191.

    Research output: Contribution to journalArticle

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    AU - MacKay, Craig

    AU - Toth, Rachel

    AU - Rouse, John

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    N2 - HLTF is highly similar in domain organisation to yeast Rad5. We identify PTIP and RPA70, both involved in DNA replication and DNA repair, as HLTF-interacting proteins although cells depleted of HLTF did not show defects in cellular responses to DNA damage. In vitro, HLTF has ATPase activity and E3 ubiquitin ligase activity with a range of E2 ubiquitin conjugating enzymes. HLTF expression is severely reduced in a range of cancer cells, and we suggest that the HLTF antibodies generated in this study could be used for cancer diagnostic purposes. (C) 2009 Elsevier Inc. All rights reserved.

    AB - HLTF is highly similar in domain organisation to yeast Rad5. We identify PTIP and RPA70, both involved in DNA replication and DNA repair, as HLTF-interacting proteins although cells depleted of HLTF did not show defects in cellular responses to DNA damage. In vitro, HLTF has ATPase activity and E3 ubiquitin ligase activity with a range of E2 ubiquitin conjugating enzymes. HLTF expression is severely reduced in a range of cancer cells, and we suggest that the HLTF antibodies generated in this study could be used for cancer diagnostic purposes. (C) 2009 Elsevier Inc. All rights reserved.

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    DO - 10.1016/j.bbrc.2009.08.151

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