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'''DSIF''' ([[5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole|DRB]] Sensitivity Inducing Factor) is a [[protein complex]] that can either negatively or positively affect transcription by [[RNA polymerase II]] (Pol II).[{{cite journal | vauthors = Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H | display-authors = 6 | title = DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs | journal = Genes & Development | volume = 12 | issue = 3 | pages = 343–356 | date = February 1998 | pmid = 9450929 | pmc = 316480 | doi = 10.1101/gad.12.3.343 }}] It can interact with the [[negative elongation factor]] (NELF) to promote the stalling of Pol II at some genes, which is called promoter proximal pausing.[{{Cite journal |last1=Tettey |first1=Theophilus T. |last2=Gao |first2=Xin |last3=Shao |first3=Wanqing |last4=Li |first4=Hua |last5=Story |first5=Benjamin A. |last6=Chitsazan |first6=Alex D. |last7=Glaser |first7=Robert L. |last8=Goode |first8=Zach H. |last9=Seidel |first9=Christopher W. |last10=Conaway |first10=Ronald C. |last11=Zeitlinger |first11=Julia |last12=Blanchette |first12=Marco |last13=Conaway |first13=Joan W. |date=2019-06-25 |title=A Role for FACT in RNA Polymerase II Promoter-Proximal Pausing |journal=Cell Reports |language=en |volume=27 |issue=13 |pages=3770–3779.e7 |doi=10.1016/j.celrep.2019.05.099|doi-access=free |pmid=31242411 }}] The pause occurs soon after initiation, once 20–60 nucleotides have been transcribed.[{{Cite journal |last1=Wen |first1=Y. |last2=Shatkin |first2=A. J. |date=1999-07-15 |title=Transcription elongation factor hSPT5 stimulates mRNA capping |journal=Genes & Development |language=en |volume=13 |issue=14 |pages=1774–1779 |doi=10.1101/gad.13.14.1774 |issn=0890-9369|doi-access=free |pmid=10421630 |pmc=316881 }}] |
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'''DSIF''' ([[5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole|DRB]] Sensitivity Inducing Factor) is a [[protein complex]] that can either negatively or positively affect transcription by [[RNA polymerase II]] (Pol II).[{{cite journal | vauthors = Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H | display-authors = 6 | title = DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs | journal = Genes & Development | volume = 12 | issue = 3 | pages = 343–356 | date = February 1998 | pmid = 9450929 | pmc = 316480 | doi = 10.1101/gad.12.3.343 }}] It can interact with the [[negative elongation factor]] (NELF) to promote the stalling of Pol II at some genes, which is called promoter proximal pausing.[{{Cite journal |last1=Tettey |first1=Theophilus T. |last2=Gao |first2=Xin |last3=Shao |first3=Wanqing |last4=Li |first4=Hua |last5=Story |first5=Benjamin A. |last6=Chitsazan |first6=Alex D. |last7=Glaser |first7=Robert L. |last8=Goode |first8=Zach H. |last9=Seidel |first9=Christopher W. |last10=Conaway |first10=Ronald C. |last11=Zeitlinger |first11=Julia |last12=Blanchette |first12=Marco |last13=Conaway |first13=Joan W. |date=2019-06-25 |title=A Role for FACT in RNA Polymerase II Promoter-Proximal Pausing |journal=Cell Reports |language=en |volume=27 |issue=13 |pages=3770–3779.e7 |doi=10.1016/j.celrep.2019.05.099|doi-access=free |pmid=31242411 }}] The pause occurs soon after initiation, once 20–60 nucleotides have been transcribed.[{{Cite journal |last1=Wen |first1=Y. |last2=Shatkin |first2=A. J. |date=1999-07-15 |title=Transcription elongation factor hSPT5 stimulates mRNA capping |journal=Genes & Development |language=en |volume=13 |issue=14 |pages=1774–1779 |doi=10.1101/gad.13.14.1774 |issn=0890-9369|doi-access=free |pmid=10421630 |pmc=316881 }}] |
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SPT5 is preserved in humans to bacteria.[{{Cite journal |last=Decker |first=Tim-Michael |date=2021-07-09 |title=Mechanisms of Transcription Elongation Factor DSIF (Spt4–Spt5) |url=https://linkinghub.elsevier.com/retrieve/pii/S0022283620305581 |journal=Journal of Molecular Biology |language=en |volume=433 |issue=14 |article-number=166657 |doi=10.1016/j.jmb.2020.09.016|pmid=32987031 |url-access=subscription }}] SPT4 and SPT5 in yeast are the homologs of hSPT4 and hSPT5.[{{Cite journal |last1=Wenzel |first1=Sabine |last2=Schweimer |first2=Kristian |last3=Rösch |first3=Paul |last4=Wöhrl |first4=Birgitta M. |date=2008-06-06 |title=The small hSpt4 subunit of the human transcription elongation factor DSIF is a Zn-finger protein with α/β type topology |url=https://linkinghub.elsevier.com/retrieve/pii/S0006291X08005640 |journal=Biochemical and Biophysical Research Communications |language=en |volume=370 |issue=3 |pages=414–418 |doi=10.1016/j.bbrc.2008.03.080|pmid=18373978 |bibcode=2008BBRC..370..414W |url-access=subscription }}] In bacteria, the homologous complex only contains ''NusG'', a Spt5 homolog.[{{Cite journal |last1=Yakhnin |first1=Alexander V. |last2=Murakami |first2=Katsuhiko S. |last3=Babitzke |first3=Paul |date=2016-03-04 |title=NusG Is a Sequence-specific RNA Polymerase Pause Factor That Binds to the Non-template DNA within the Paused Transcription Bubble |journal=Journal of Biological Chemistry |language=en |volume=291 |issue=10 |pages=5299–5308 |doi=10.1074/jbc.M115.704189|doi-access=free |pmid=26742846 |pmc=4777861 }}] Archaea have both proteins.[{{cite journal | vauthors = Fouqueau T, Blombach F, Cackett G, Carty AE, Matelska DM, Ofer S, Pilotto S, Phung DK, Werner F | display-authors = 6 | title = The cutting edge of archaeal transcription | journal = Emerging Topics in Life Sciences | volume = 2 | issue = 4 | pages = 517–533 | date = December 2018 | pmid = 33525828 | pmc = 7289017 | doi = 10.1042/ETLS20180014 | doi-access = free }}] |
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SPT5 is preserved in humans to bacteria.[{{Cite journal |last=Decker |first=Tim-Michael |date=2021-07-09 |title=Mechanisms of Transcription Elongation Factor DSIF (Spt4–Spt5) |url=https://linkinghub.elsevier.com/retrieve/pii/S0022283620305581 |journal=Journal of Molecular Biology |language=en |volume=433 |issue=14 |article-number=166657 |doi=10.1016/j.jmb.2020.09.016|pmid=32987031 |url-access=subscription }}] SPT4 and SPT5 in yeast are the homologs of hSPT4 and hSPT5.[{{Cite journal |last1=Wenzel |first1=Sabine |last2=Schweimer |first2=Kristian |last3=Rösch |first3=Paul |last4=Wöhrl |first4=Birgitta M. |date=2008-06-06 |title=The small hSpt4 subunit of the human transcription elongation factor DSIF is a Zn-finger protein with α/β type topology |url=https://linkinghub.elsevier.com/retrieve/pii/S0006291X08005640 |journal=Biochemical and Biophysical Research Communications |language=en |volume=370 |issue=3 |pages=414–418 |doi=10.1016/j.bbrc.2008.03.080|pmid=18373978 |bibcode=2008BBRC..370..414W |url-access=subscription }}] In bacteria, the homologous complex only contains ''NusG'', a Spt5 homolog.[{{Cite journal |last1=Yakhnin |first1=Alexander V. |last2=Murakami |first2=Katsuhiko S. |last3=Babitzke |first3=Paul |date=2016-03-04 |title=NusG Is a Sequence-specific RNA Polymerase Pause Factor That Binds to the Non-template DNA within the Paused Transcription Bubble |journal=Journal of Biological Chemistry |language=en |volume=291 |issue=10 |pages=5299–5308 |doi=10.1074/jbc.M115.704189|doi-access=free |pmid=26742846 |pmc=4777861 }}] [[Archaea]] have both proteins.[{{cite journal | vauthors = Fouqueau T, Blombach F, Cackett G, Carty AE, Matelska DM, Ofer S, Pilotto S, Phung DK, Werner F | display-authors = 6 | title = The cutting edge of archaeal transcription | journal = Emerging Topics in Life Sciences | volume = 2 | issue = 4 | pages = 517–533 | date = December 2018 | pmid = 33525828 | pmc = 7289017 | doi = 10.1042/ETLS20180014 | doi-access = free }}] |
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The complex locks the RNA polymerase (RNAP) clamp into a closed state to prevent the elongation complex (EC) from dissociating. The Spt5 [[NGN domain]] helps anneal the two strands of DNA upstream. The single [[KOW domain]] in bacteria and archaea anchors a [[ribosome]] to the RNAP. |
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The complex locks the RNA polymerase (RNAP) clamp into a closed state to prevent the elongation complex (EC) from dissociating. The Spt5 [[NGN domain]] helps anneal the two strands of DNA upstream. The single [[KOW domain]] in bacteria and archaea anchors a [[ribosome]] to the RNAP. |
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DSIF plays the same role for HIV-1 gene expression as it would normally in transcription.[{{Cite journal |last1=Zhang |first1=Zhiqiang |last2=Klatt |first2=Alicia |last3=Gilmour |first3=David S. |last4=Henderson |first4=Andrew J. |date=2007-06-08 |title=Negative Elongation Factor NELF Represses Human Immunodeficiency Virus Transcription by Pausing the RNA Polymerase II Complex |journal=Journal of Biological Chemistry |language=en |volume=282 |issue=23 |pages=16981–16988 |doi=10.1074/jbc.M610688200|doi-access=free |pmid=17442680 }}][{{Cite journal |last1=Ping |first1=Yueh-Hsin |last2=Rana |first2=Tariq M. |date=2001-04-20 |title=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 |journal=Journal of Biological Chemistry |language=en |volume=276 |issue=16 |pages=12951–12958 |doi=10.1074/jbc.M006130200|doi-access=free |pmid=11112772 }}] This is because P-TEFb phosphorylates DSIF the same regardless of whether or not P-TEFb goes through normal cellular regulation or bypasses it due to [[Tat (HIV)|Tat]].[{{Cite journal |last1=Zhu |first1=Yuerong |last2=Pe’ery |first2=Tsafrira |last3=Peng |first3=Junmin |last4=Ramanathan |first4=Yegnanarayana |last5=Marshall |first5=Nick |last6=Marshall |first6=Tricia |last7=Amendt |first7=Brad |last8=Mathews |first8=Michael B. |last9=Price |first9=David H. |date=1997-10-15 |title=Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro |journal=Genes & Development |language=en |volume=11 |issue=20 |pages=2622–2632 |doi=10.1101/gad.11.20.2622 |issn=0890-9369|doi-access=free |pmid=9334325 |pmc=316609 }}] |
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DSIF plays the same role for HIV-1 [[gene expression]] as it would normally in transcription.[{{Cite journal |last1=Zhang |first1=Zhiqiang |last2=Klatt |first2=Alicia |last3=Gilmour |first3=David S. |last4=Henderson |first4=Andrew J. |date=2007-06-08 |title=Negative Elongation Factor NELF Represses Human Immunodeficiency Virus Transcription by Pausing the RNA Polymerase II Complex |journal=Journal of Biological Chemistry |language=en |volume=282 |issue=23 |pages=16981–16988 |doi=10.1074/jbc.M610688200|doi-access=free |pmid=17442680 }}][{{Cite journal |last1=Ping |first1=Yueh-Hsin |last2=Rana |first2=Tariq M. |date=2001-04-20 |title=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 |journal=Journal of Biological Chemistry |language=en |volume=276 |issue=16 |pages=12951–12958 |doi=10.1074/jbc.M006130200|doi-access=free |pmid=11112772 }}] This is because P-TEFb [[Phosphorylation|phosphorylates]] DSIF the same regardless of whether or not P-TEFb goes through normal cellular regulation or bypasses it due to [[Tat (HIV)|Tat]].[{{Cite journal |last1=Zhu |first1=Yuerong |last2=Pe’ery |first2=Tsafrira |last3=Peng |first3=Junmin |last4=Ramanathan |first4=Yegnanarayana |last5=Marshall |first5=Nick |last6=Marshall |first6=Tricia |last7=Amendt |first7=Brad |last8=Mathews |first8=Michael B. |last9=Price |first9=David H. |date=1997-10-15 |title=Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro |journal=Genes & Development |language=en |volume=11 |issue=20 |pages=2622–2632 |doi=10.1101/gad.11.20.2622 |issn=0890-9369|doi-access=free |pmid=9334325 |pmc=316609 }}] |
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