The Paf1 Complex Is Required for Histone H3 Methylation by COMPASS and Dot1p: Linking Transcriptional Elongation to Histone Methylation

Krogan, Nevan J.; Dover, Jim; Wood, Adam; Schneider, Jessica; Heidt, Jonathan; Boateng, Marry Ann; Dean, Kimberly; Ryan, Owen; Golshani, Ashkan; Johnston, Mark; Greenblatt, Jack; Shilatifard, Ali

doi:10.1016/s1097-2765(03)00091-1

Cited by 666 publications

(733 citation statements)

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“…It was initially demonstrated in yeast that COMPASS and H3K4 methylation are localized to punctuate sites near the transcription start sites for actively transcribed genes [32,33]. This H3K4 localization pattern also holds true in higher eukaryotic organisms including mammals [34].…”

Section: H3k4 Methylation Distribution Pattern Throughout the Genomementioning

confidence: 92%

“…The methyltransferase function of MLLs in human are non-redundant as deletion of either MLLs result in embryonic lethality. Previous studies demonstrated that COMPASS interacts with the elongating form of Pol II via its interaction with the Paf1 complex [32,43]. Therefore, (A) in the absence of H2B monoubiquitination, COMPASS can still interact with the transcribing Pol II via the Paf1 complex and monomethylate H3K4.…”

Section: Figure 2 Subunit Composition For Compass In Yeast and Its Hmentioning

confidence: 98%

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Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation

Shilatifard

2008

Current Opinion in Cell Biology

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437

408

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Chromosomal surfaces are ornamented with a variety of posttranslational modifications of histones, which are required for the regulation of many of the DNA-templated processes. Such histone modifications include acetylation, sumoylation, phosphorylation, ubiquitination and methylation. Histone modifications can either function by disrupting chromosomal contacts or by regulating nonhistone protein interactions with chromatin. In this review, recent findings will be discussed regarding the regulation of the implementation and physiological significance for one such histone modification, histone H3 Lysine 4 (H3K4) methylation by the yeast COMPASS and mammalian COMPASS-like complexes.All DNA-templated processes are regulated by chromatin and its posttranslational modifications. The nucleosome, which is the fundamental unit of chromatin, is composed of 146 base pairs of DNA wrapped twice around an octamer of the four core histones (H3, H4, H2A, and H2B) [1][2][3]. Structural studies demonstrated that the unstructured histone N-terminal tails protrude outward from the nucleosomes and are available for interactions with other neighboring histones or non-histone proteins. Many residues within the histone N-terminal tails and a few within the histone core can be altered by posttranslational modifications [1]. To date, there are at least five types of posttranslational modifications found on histones, these include: acetylation, phosphorylation, ubiquitination, sumoylation, and methylation [4,5]. Almost all of these modifications have been shown to be reversible, and their implementation and removal are fundamental to the regulation of a diverse set of biological processes such as replication, repair, recombination, transcription and RNA processing [4,5]. This review will focus mainly on the most recent studies of one type of histone modification, histone H3 lysine 4 (H3K4) methylation. Histone lysine methylationHistones are methylated either on their arginine and/or lysine residues [6,7]. The lysine residues are methylated on the ε-nitrogen by either the SET domain or the non-SET domain-containing lysine methyltransferases (KMTs). A large number of enzymes have been characterized which are capable of methylating specific lysine residues on histones ( Table 1). The ε-nitrogen can also be modified by lysine acetyl transferases (KATs) and methylation and acetylation of lysine are mutually exclusive. Indeed, many sites of histone methylation are also sites of acetylation.Correspondence and proofs should be sent to the following address: Ali Shilatifard, Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, Office (816) 926-4465, Email: ASH@Stowers-Institute.org. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable for...

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Section: H3k4 Methylation Distribution Pattern Throughout the Genomementioning

confidence: 92%

Section: Figure 2 Subunit Composition For Compass In Yeast and Its Hmentioning

confidence: 98%

Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation

Shilatifard

2008

Current Opinion in Cell Biology

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437

408

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“…Therefore, yPAF was postulated to be involved in both RNA polymerase IImediated transcription initiation and elongation. Recently, the yPAF complex has been shown to be required for Rad6-mediated histone H2B-K123 monoubiquitination (Ng et al 2003b;Wood et al 2003), Set1-mediated histone H3-K4 methylation (Krogan et al 2003;Ng et al 2003a), and Dot1-mediated histone H3-K79 methylation (Krogan et al 2003), placing PAF at the center of cotranscriptional histone modifications (for review, see Hampsey and Reinberg 2003). PAF subunits are also required for maintaining proper poly(A) tail length in yeast, suggesting a post-transcriptional role for PAF complex in mRNA processing and maturation (Mueller et al 2004).…”

mentioning

confidence: 99%

The human PAF complex coordinates transcription with events downstream of RNA synthesis

Zhu¹,

Mandal²,

Pham³

et al. 2005

Genes Dev.

209

236

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The yeast PAF (yPAF) complex interacts with RNA polymerase II and coordinates the setting of histone marks associated with active transcription. We report the isolation and functional characterization of the human PAF (hPAF) complex. hPAF shares four subunits with yPAF (hCtr9, hPaf1, hLeo1, and hCdc73), but contains a novel higher eukaryotic-specific subunit, hSki8. RNAi against hSki8 or hCtr9 reduces the cellular levels of other hPAF subunits and of mono-and trimethylated H3-Lys 4 and dimethylated H3-Lys 79. The hSki8 subunit is also a component of the human SKI (hSKI) complex. Yeast SKI complex is cytoplasmic and together with Exosome mediates 3 -5 mRNA degradation. However, hSKI complex localizes to both nucleus and cytoplasm. Immunoprecipitation experiments revealed that hPAF and hSKI complexes interact, and ChIP experiments demonstrated that hSKI associates with transcriptionally active genes dependent on the presence of hPAF. Thus, in addition to coordinating events during transcription (initiation, promoter clearance, and elongation), hPAF also coordinates events in RNA quality control.Supplemental material is available at http://www.genesdev.org.

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“…Several important predictions arising from this E-MAP for novel gene functions have recently been studied and confirmed (10)(11)(12)(13)(14)(15)(16)(17). One such prediction was a connection between SET2, a histone methyltransferase, and Rpd3C(S), a histone deacetylation complex that contains the chromodomain protein Eaf3p as well as Rco1p.…”

Section: Introductionmentioning

confidence: 76%

Quantitative genetic analysis in Saccharomyces cerevisiae using epistatic miniarray profiles (E-MAPs) and its application to chromatin functions

Schuldiner

Collins

Weissman

et al. 2006

Methods

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The use of the budding yeast Saccharomyces cerevisiae as a simple eukaryotic model system for the study of chromatin assembly and regulation has allowed rapid discovery of genes that influence this complex process. The functions of many of the proteins encoded by these geneshave not yet been fully characterized. Here, we describe a high-throughput methodology that can be used to illuminate gene function and discuss its application to a set of genes involved in the creation, maintenance and remodeling of chromatin structure. Our technique, termed EMAPs, involves the generation of quantitative genetic interaction maps that reveal the function and organization of cellular proteins and networks.

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The Paf1 Complex Is Required for Histone H3 Methylation by COMPASS and Dot1p: Linking Transcriptional Elongation to Histone Methylation

Cited by 666 publications

References 45 publications

Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation

Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation

The human PAF complex coordinates transcription with events downstream of RNA synthesis

Quantitative genetic analysis in Saccharomyces cerevisiae using epistatic miniarray profiles (E-MAPs) and its application to chromatin functions

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