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  Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop

Lee, Y., Yoon, E., Cho, S., Schmähling, S., Müller, J., & Song, J.-J. (2019). Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop. Structure, 27(5), 846-852.e3. doi:10.1016/j.str.2019.01.016.

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 Creators:
Lee, Yoonjung1, Author
Yoon, Eojin1, Author
Cho, Saehyun1, Author
Schmähling, Sigrun2, Author              
Müller, Jürg2, Author              
Song, Ji-Joon1, Author
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1external, ou_persistent22              
2Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565161              

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Free keywords: NURD COMPLEX; METHYLATION; RECOGNITION; DOMAIN; H4Biochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: Human ASH1L is the catalytic subunit of the conserved histone methyltransferase (HMTase) complex AMC that dimethylates lysine 36 in histone H3 (H3K36me2) to promote gene transcription in mammals and flies. Unlike AMC, ASH1L alone shows poor catalytic activity, because access to its substrate binding pocket is blocked by an autoinhibitory loop (AI loop) from the postSET domain. We report the crystal structure of the minimal catalytic active AMC complex containing ASH1L and its partner subunit MRG15. The structure reveals how binding of the MRG domain of MRG15 to a conserved FxLP motif in ASH1L results in the displacement of the AI loop to permit substrates to access the catalytic pocket of the ASH1L SET domain. Together, ASH1L activation by MRG15 therefore represents a delicate regulatory mechanism for how a cofactor activates an SET domain HMTase by releasing autoinhibition.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000467238900014
DOI: 10.1016/j.str.2019.01.016
 Degree: -

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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 27 (5) Sequence Number: - Start / End Page: 846 - 852.e3 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1