COMPASS: A complex of proteins associated with a trithorax-related SET domain protein

By Trissa Miller, Nevan J. Krogan, J. Dover, H. Erdjument‐Bromage, Paul Tempst, Mark Johnston, Jack Greenblatt, A. Shilatifard. Proceedings of the National Academy of Sciences of the United States of America, 2001

648 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/5c191298784bc7f38748957e1234dad788734d1c

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

Leukemia Proto-Oncoprotein MLL Forms a SET1-Like Histone Methyltransferase Complex with Menin To Regulate Hox Gene Expression (2004, methodology): “The composition of MLL/HCF shares considerable similarity with the previously characterized SET1 HMT complexes of Saccharomyces cerevisiae and humans (41, 43, 47, 61) (Fig.”
The interplay of histone modifications – writers that read (2015, positive): “These complexes are comprised of the catalytic SETD1/ MLL subunits and four core subunits WDR5, RBBP5, ASH2L, and DPY30, and as well many other complex-specific subunits [13 – 15].”
Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. (2003, background): “Genetic (Nislow et al., Swi/Snf, Isw2, RSC) can be recruited by specific activa- 1997) and transcriptional profiling (Miller et al., 2001; tors or repressors, depending on the promoter (Cosma Bernstein et al., 2002) experiments have identified genes et al., 1999; Agalioti et al., 2000; Goldmark et…”
The COMPASS Family of Histone H3K4 Methylases: Mechanisms of Regulation in Development and Disease Pathogenesis (2012, methodology): “It has been almost ten years since the original report on the biochemical purification of Set1/ COMPASS as the yeast homolog of Drosophila trx and mammalian MLL (42) and its”
Methylation of Histone H3 by Set2 in Saccharomyces cerevisiae Is Linked to Transcriptional Elongation by RNA Polymerase II (2003, background): “COMPASS methylates Lys4 of histone H3, a modification that has been shown to be needed for effective silencing at telomeres and ribosomal DNA loci (7, 24, 33, 36, 46).”
WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. (2005, positive): “lated human proteins, hSet1, MLL1, and MLL2, all of which are capable of methylating H3 at K4 (Roguev et al., 2001; Miller et al., 2001; Nagy et al., 2002; Milne et al., 2002; Nakamura et al., 2002; Wysocka et al., 2003; Hughes et al., 2004; Yokoyama et al., 2004).”
Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. (2006, background): “Set1 and Set2 methylate lysines 4 and 36 of histone H3, respectively, and both of these marks are associated with active genes (Briggs et al., 2001; Miller et al., 2001; Li et al., 2002; Nagy et al., 2002; Noma and Grewal, 2002; Krogan et al., 2003b; Schaft et al., 2003).”
A chromatin landmark and transcription initiation at most promoters in human cells. (2007, background): “The histone methyltransferase (HMT) responsible for H3K4me3 modiﬁcation in yeast, the Set1 complex, is recruited to the 5 0 end of actively transcribed genes by interacting with the RNA polymerase II (Pol II)- associated PAF complex (Miller et al., 2001; Krogan et al., 2003a; Laribee et al., 2005).”
Elongation by RNA polymerase II: the short and long of it. (2004, background): “Set1 functions as a specific histone H3-K4 methyltransferase in yeast and copurifies with a large complex (Briggs et al. 2001; Miller et al. 2001; Roguev et al. 2001; Krogan et al. 2002a; Nagy et al. 2002; Noma and Grewal 2002).”
Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. (2002, background): “complex isolated from yeast (Miller et al. 2001) was able to methylate this residue in vitro.”