Transcription elongation factor SPT5

Definition

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.

References:

[1]. Y Wen, et al. Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev. 1999 Jul 15;13(14):1774-9. [Content Brief]

[2]. J B Kim, et al. Tat-SF1 protein associates with RAP30 and human SPT5 proteins. Mol Cell Biol. 1999 Sep;19(9):5960-8. [Content Brief]

[3]. D B Renner, et al. A highly purified RNA polymerase II elongation control system. J Biol Chem. 2001 Nov 9;276(45):42601-9. [Content Brief]

[4]. Y Yamaguchi, et al. Structure and function of the human transcription elongation factor DSIF. J Biol Chem. 1999 Mar 19;274(12):8085-92. [Content Brief]

[5]. D Ivanov, et al. Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Mol Cell Biol. 2000 May;20(9):2970-83. [Content Brief]

[6]. C A Parada, et al. A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 1999 Jul 1;18(13):3688-701. [Content Brief]

[7]. F Wu-Baer, et al. Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation. J Mol Biol. 1998 Mar 27;277(2):179-97. [Content Brief]

[8]. Y Yamaguchi, et al. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell. 1999 Apr 2;97(1):41-51. [Content Brief]

[9]. Barbara H Jennings, et al. Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila. Curr Biol. 2004 Sep 21;14(18):1680-4. [Content Brief]

[10]. T Wada, et al. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J. 1998 Dec 15;17(24):7395-403. [Content Brief]

[11]. Youn Tae Kwak, et al. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell. 2003 Apr;11(4):1055-66. [Content Brief]

[12]. T Wada, et al. FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH. Mol Cell. 2000 Jun;5(6):1067-72. [Content Brief]

[13]. Cyril F Bourgeois, et al. Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences. Mol Cell Biol. 2002 Feb;22(4):1079-93. [Content Brief]

[14]. T Wada, et al. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. Genes Dev. 1998 Feb 1;12(3):343-56. [Content Brief]

[15]. Murali Palangat, et al. A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS. Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15036-41. [Content Brief]

[16]. Dong-Ki Kim, et al. Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex. Genes Cells. 2003 Apr;8(4):371-8. [Content Brief]

[17]. Koh Fujinaga, et al. Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Mol Cell Biol. 2004 Jan;24(2):787-95. [Content Brief]

[18]. Subhrangsu S Mandal, et al. Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7572-7. [Content Brief]

[19]. Y H Ping, et al. DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation. J Biol Chem. 2001 Apr 20;276(16):12951-8. [Content Brief]

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