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    Home > Biochemistry News > Biotechnology News > A novel mechanism for the regulation of proline hydroxylase EGLN1 activity

    A novel mechanism for the regulation of proline hydroxylase EGLN1 activity

    • Last Update: 2022-08-11
    • Source: Internet
    • Author: User
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    EGLN1 plays a crucial biological function in HIF-mediated hypoxia signaling pathway, however, the regulation of EGLN1 activity and its molecular mechanism are still uncle.


    This study showed that SET7 directly binds and methylates EGLN1, inhibiting its hydroxylase activity, but does not affect the stability of EGLN1 prote.


    In addition, the team's earlier research results showed that the methyltransferase SET7 can also directly methylate and modify the hypoxia-inducible factor HIF-α, regulating its ability to bind to the promoters of genes downstream of hypoxia, thereby regulating HIF under hypoxia stre.


    These studies not only reveal the precise regulation of SET7-mediated lysine methylation on hypoxia response and hypoxia tolerance, but also provide potential molecular targets for the breeding of new hypoxia-tolerant fish speci.


    This study was recently published online in the Journal of Biological Chemistry (Tang et al , 2022)under the title EGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1α is repressed by SET7-catalyzed lysine methylati.


    Paper link: https://d.


    The mode of action of SET7-mediated methylation modification in regulating hypoxia signaling pathway 

    Identification of lysine methylation modification sites of EGLN1 by mass spectrometry

    Conservation of EGLN1 methylation modification sites

    Knockout of SET7 enhances hypoxia tolerance in fish

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