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Protein interactions within the SET1 complex and their roles in the regulation of histone 3 lysine 4 methylation

Dehe, Pierre-Marie, Dichtl, Bernhard, Schaft, Daniel, Roguev, Assen, Pamblanco, Merce, Lebrun, Régine, Rodríguez-Gil, Alfonso, Mkandawire, Msau, Landsberg, Katarina, Shevchenko, Anna, Shevchenko, Andrej, Rosaleny, Lorena E., Tordera, Vicente, Chávez, Sebastián and Géli, Vincent 2006, Protein interactions within the SET1 complex and their roles in the regulation of histone 3 lysine 4 methylation, Journal of biological chemistry, vol. 281, no. 46, pp. 35404-35412, doi: 10.1074/jbc.M603099200.

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Title Protein interactions within the SET1 complex and their roles in the regulation of histone 3 lysine 4 methylation
Author(s) Dehe, Pierre-Marie
Dichtl, BernhardORCID iD for Dichtl, Bernhard orcid.org/0000-0001-5514-4982
Schaft, Daniel
Roguev, Assen
Pamblanco, Merce
Lebrun, Régine
Rodríguez-Gil, Alfonso
Mkandawire, Msau
Landsberg, Katarina
Shevchenko, Anna
Shevchenko, Andrej
Rosaleny, Lorena E.
Tordera, Vicente
Chávez, Sebastián
Géli, Vincent
Journal name Journal of biological chemistry
Volume number 281
Issue number 46
Start page 35404
End page 35412
Publisher American Society for Biochemistry and Molecular Biology
Place of publication Baltimore, Md
Publication date 2006-11-17
ISSN 0021-9258
1083-351X
Summary Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc1 strongly interacts with itself. Inactivation of either Bre2 or Sdc1 has very similar effects. Neither is required for complex integrity, and their removal results in an increase of H3K4 mono- and dimethylation and a severe decrease of trimethylation at the 5′ end of active coding regions but a decrease of H3K4 dimethylation at the 3′ end of coding regions. Cells lacking Spp1 have a reduced amount of Set1 and retain a fraction of trimethylated H3K4, whereas cells lacking Shg1 show slightly elevated levels of both di- and trimethylation. Set1C associates with both serine 5- and serine 2-phosphorylated forms of polymerase II, indicating that the association persists to the 3′ end of transcribed genes. Taken together, our results suggest that Set1C subunits stimulate Set1 catalytic activity all along active genes.
Language eng
DOI 10.1074/jbc.M603099200
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2006, American Society for Biochemistry and Molecular Biology
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039335

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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