Kinetic Manifestation of Processivity during Multiple Methylations Catalyzed by SET Domain Protein Methyltransferases†

Biochemistry ◽  
2007 ◽  
Vol 46 (12) ◽  
pp. 3905-3915 ◽  
Author(s):  
Lynnette M. A. Dirk ◽  
E. Megan Flynn ◽  
Kevin Dietzel ◽  
Jean-François Couture ◽  
Raymond C. Trievel ◽  
...  
Keyword(s):  
Set Domain ◽  
Domain Protein ◽  
Protein Methyltransferases

scholarly journals Strategy to Target the Substrate Binding site of SET Domain Protein Methyltransferases

2013 ◽  
Vol 53 (3) ◽  
pp. 681-691 ◽  
Author(s):  
Kong T. Nguyen ◽  
Fengling Li ◽  
Gennadiy Poda ◽  
David Smil ◽  
Masoud Vedadi ◽  
...  
Keyword(s):  
Binding Site ◽  
Substrate Binding ◽  
Set Domain ◽  
Substrate Binding Site ◽  
Domain Protein ◽  
Protein Methyltransferases

scholarly journals Structural origins for the product specificity of SET domain protein methyltransferases

2008 ◽  
Vol 105 (52) ◽  
pp. 20659-20664 ◽  
Author(s):  
J.-F. Couture ◽  
L. M. A. Dirk ◽  
J. S. Brunzelle ◽  
R. L. Houtz ◽  
R. C. Trievel
Keyword(s):  
Set Domain ◽  
Product Specificity ◽  
Domain Protein ◽  
Protein Methyltransferases

Exploring the origin of the catalytic power and product specificity of SET domain protein methyltransferase

2016 ◽  
Vol 12 (10) ◽  
pp. 2980-2983 ◽  
Author(s):  
A. H. Lima ◽  
C. N. Alves ◽  
R. Prasad ◽  
J. Lameira
Keyword(s):  
Computer Simulation ◽  
Set Domain ◽  
Product Specificity ◽  
Protein Methyltransferase ◽  
Domain Protein ◽  
Catalytic Power

Computer simulation reveals that the origin of SET8 catalytic power is mainly due to electrostatic preorganization.

scholarly journals The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair

2005 ◽  
Vol 102 (50) ◽  
pp. 18075-18080 ◽  
Author(s):  
S.-H. Lee ◽  
M. Oshige ◽  
S. T. Durant ◽  
K. K. Rasila ◽  
E. A. Williamson ◽  
...  
Keyword(s):  
Nonhomologous End Joining ◽  
Set Domain ◽  
End Joining ◽  
Dna Integration ◽  
Foreign Dna ◽  
Domain Protein ◽  
Foreign Dna Integration

scholarly journals Phylogenetic profiling suggests early origin of the core subunits of Polycomb Repressive Complex 2 (PRC2)

2021 ◽  
Author(s):  
Abdoallah Sharaf ◽  
Mallika Vijayanathan ◽  
Miroslav Obornik ◽  
iva Mozgova
Keyword(s):  
Developmental Regulation ◽  
Structural Diversity ◽  
Polycomb Group ◽  
Catalytic Subunit ◽  
Set Domain ◽  
Polycomb Repressive Complex ◽  
Polycomb Repressive Complex 2 ◽  
Domains Of Life ◽  
Domain Protein ◽  
Phylogenetic Profiling

Polycomb Repressive Complex 2 (PRC2) is involved in establishing transcriptionally silent chromatin states through its ability to methylate lysine 27 of histone H3 by the catalytic subunit Enhancer of zeste [E(z)]. Polycomb group (PcG) proteins play a crucial role in the maintenance of cell identity and in developmental regulation. Previously, the diversity of PRC2 subunits within some eukaryotic lineages has been reported and its presence in early eukaryotic evolution has been hypothesized. So far however, systematic survey of the presence of PRC2 subunits in species of all eukaryotic lineages is missing. Here, we report the diversity of PRC2 core subunit proteins in different eukaryotic supergroups with emphasis on the early-diverged lineages and explore the molecular evolution of PRC2 subunits by phylogenetics. In detail, we investigate the SET-domain protein sequences and their evolution across the four domains of life and particularly focus on the structural diversity of the SET-domain subfamily containing E(z), the catalytic subunit of PRC2. We show that PRC2 subunits are already present in early eukaryotic lineages, strengthening the support for PRC2 emergence prior to diversification of eukaryotes. We identify a common presence of E(z) and ESC, suggesting that Su(z)12 may have emerged later and/or may be dispensable from the evolutionarily conserved functional core of PRC2. Furthermore, our results broaden our understanding of the E(z) evolution within the SET-domain protein family, suggesting possibilities of function evolution. Through this, we shed light on a possible emerging point of the PRC2 and the evolution of its function in eukaryotes.

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