Human Spt6 Stimulates Transcription Elongation by RNA Polymerase II In Vitro

Endoh, Masaki; Zhu, Wenyan; Hasegawa, Jun; Watanabe, Hidenobu; Kim, Yon Su; Aida, Masao; Inukai, Naoto; Narita, Takashi; Yamada, Tomoko; Furuya, Akiko; Sato, Hitoshi; Yamaguchi, Yuki; Mandal, Subhrangsu S.; Reinberg, Danny; Wada, Tadashi; Handa, Hiroshi

doi:10.1128/mcb.24.8.3324-3336.2004

Cited by 111 publications

(113 citation statements)

References 32 publications

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“…Interaction studies showed that DSIF genetically and physically associates with TFIIF, TFIIS, and CSB (Rad26) as well as the chromatin-related factors Spt6, FACT, Chd1, and the PAF complex Orphanides et al 1999;Costa and Arndt 2000;Jansen et al 2000;Krogan et al 2002b;Mueller and Jaehning 2002;Squazzo et al 2002;Lindstrom et al 2003;Simic et al 2003;Endoh et al 2004). In addition, Spt5 interacts with factors implicated in mRNA maturation and surveillance (see below) (Wen and Shatkin 1999;Andrulis et al 2002;Pei and Shuman 2002;Lindstrom et al 2003).…”

Section: Dsifmentioning

confidence: 99%

“…This finding supports the idea that Spt6 aids in maintaining chromatin structure during elongation. Studies using classical elongation assays on naked DNA in vitro demonstrated that Spt6 functions as an elongation factor that stimulates the transcription rate of RNAP II both autonomously and together with DSIF (Endoh et al 2004). Together, these results implicate Spt6 as a modulator of RNAP II activity during elongation, as well as a maintenance factor for chromatin structure.…”

Section: Spt6mentioning

confidence: 99%

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Elongation by RNA polymerase II: the short and long of it

Sims¹,

Belotserkovskaya²,

Reinberg³

2004

Genes Dev.

Self Cite

614

586

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Appreciable advances into the process of transcript elongation by RNA polymerase II (RNAP II) have identified this stage as a dynamic and highly regulated step of the transcription cycle. Here, we discuss the many factors that regulate the elongation stage of transcription. Our discussion includes the classical elongation factors that modulate the activity of RNAP II, and the more recently identified factors that facilitate elongation on chromatin templates. Additionally, we discuss the factors that associate with RNAP II, but do not modulate its catalytic activity. Elongation is highlighted as a central process that coordinates multiple stages in mRNA biogenesis and maturation.The regulation of gene expression is one of the most intensely studied areas in all of science. Differential gene expression in multicellular organisms forms the foundation of cell-type specificity. Deregulation of the appropriate pattern of gene expression has profound effects on cellular function and underlies many diseases. Although there are many cellular processes that control gene expression, the most direct regulation occurs during transcription. The transcription of protein-coding genes in eukaryotes is performed by RNA polymerase II (RNAP II). Up until recently, the vast majority of studies aimed at elucidating the molecular mechanisms of transcription regulation have focused on early stages, such as the formation of a transcription initiation complex (preinitiation) and initiation (see below). For many years, transcript elongation has been thought of as the trivial addition of ribonucleoside triphosphates to the growing mRNA chain. It is now apparent that this process is a dynamic and highly regulated stage of the transcription cycle capable of coordinating downstream events. Numerous factors have been identified that specifically target the elongation stage of transcription. Importantly, multiple steps in mRNA maturation, including premRNA capping, splicing, 3Ј-end processing, surveillance, and export, are modulated through interactions with the RNAP II transcript elongation complex (TEC). It also appears that distinct elongation factors function in specific transcriptional contexts; the requirements for these specialized factors are largely unknown and highlight the need to better understand elongation in vivo. Many molecular and biochemical approaches have been used to quantify the different aspects of elongation, many of which are discussed below. It remains important to assimilate both in vitro and in vivo experimental systems when discussing what constitutes an elongation factor. An elongation factor can be defined as any molecule that affects the activities of or is associated with the TEC. We suggest that there are at least two major types of transcript elongation factors: one family, referred to as active elongation factors, and a second family, denoted as passive elongation factors. The difference resides in whether the factor affects the catalytic activity of RNAP II, regardless of whether the factor remains associate...

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Section: Dsifmentioning

confidence: 99%

Section: Spt6mentioning

confidence: 99%

Elongation by RNA polymerase II: the short and long of it

Sims¹,

Belotserkovskaya²,

Reinberg³

2004

Genes Dev.

Self Cite

614

586

View full text Add to dashboard Cite

show abstract

“…1 Spt6 was later described as an essential nuclear protein. 2,3 Like Spt4 and Spt5, Spt6 is required for transcription elongation, 4,5,31,70 and co-localizes with Spt5 and RNA polymerase (Pol) II at transcriptionally active loci on Drosophila polytene chromosomes. 6,7 Spt6 interacts with the structured part of histone H3 and can deposit nucleosomes on DNA in a supercoiling assay.…”

Section: Introductionmentioning

confidence: 99%

Structure and in Vivo Requirement of the Yeast Spt6 SH2 Domain

Dengl

Mayer

Sun

et al. 2009

Journal of Molecular Biology

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During transcription elongation through chromatin, the Ser2-phosphorylated C-terminal repeat domain of RNA polymerase II binds the C-terminal Src homology 2 (SH2) domain of the nucleosome re-assembly factor Spt6. This SH2 domain is unusual in its specificity to bind phosphoserine, rather than phosphotyrosine and because it is the only SH2 domain in the yeast genome. Here, we report the high-resolution crystal structure of the SH2 domain from Candida glabrata Spt6. The structure combines features from both structural subfamilies of SH2 domains, suggesting it resembles a common ancestor of all SH2 domains. Two conserved surface pockets deviate from those of canonical SH2 domains, and may explain the unusual phosphoserine specificity. Differential gene expression analysis reveals that the SH2 domain is required for normal expression of a subset of yeast genes, and is consistent with multiple functions of Spt6 in chromatin transcription.

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“…Spt6 activates transcription elongation of many genes in vivo (11,(13)(14)(15), regulates histone H3 lysine 36 methylation, and participates in mRNA 3Ј-end processing and export (16 -18). Many research reports have indicated that Spt6 cooperates with another histone H2A⅐H2B chaperone named FACT (FAcilitates Chromatin Transcription) in the reassembly of chromatin in the wake of transcribing RNAPII (12, 19 -21).…”

mentioning

confidence: 99%