6gml

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==Structure of paused transcription complex Pol II-DSIF-NELF==
==Structure of paused transcription complex Pol II-DSIF-NELF==
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<StructureSection load='6gml' size='340' side='right' caption='[[6gml]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='6gml' size='340' side='right'caption='[[6gml]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6gml]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GML FirstGlance]. <br>
<table><tr><td colspan='2'>[[6gml]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GML FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/NELFA_HUMAN NELFA_HUMAN]] Wolf-Hirschhorn syndrome.
[[http://www.uniprot.org/uniprot/NELFA_HUMAN NELFA_HUMAN]] Wolf-Hirschhorn syndrome.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RPB9_PIG RPB9_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). [[http://www.uniprot.org/uniprot/NELFE_HUMAN NELFE_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex.<ref>PMID:10199401</ref> <ref>PMID:11940650</ref> <ref>PMID:12612062</ref> [[http://www.uniprot.org/uniprot/I3LGP4_PIG I3LGP4_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031] [[http://www.uniprot.org/uniprot/SPT4H_HUMAN SPT4H_HUMAN]] 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 [[http://www.uniprot.org/uniprot/NELFD_HUMAN NELFD_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex.<ref>PMID:10199401</ref> <ref>PMID:12612062</ref> [[http://www.uniprot.org/uniprot/I3LCB2_PIG I3LCB2_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.[PIRNR:PIRNR000779] [[http://www.uniprot.org/uniprot/NELFA_HUMAN NELFA_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. Probably required to interact with the RNA polymerase II complex.<ref>PMID:10199401</ref> <ref>PMID:12563561</ref> <ref>PMID:12612062</ref> [[http://www.uniprot.org/uniprot/NELFB_HUMAN NELFB_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, binds weakly to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1. May be able to induce chromatin unfolding.<ref>PMID:10199401</ref> <ref>PMID:12612062</ref> <ref>PMID:23884411</ref> <ref>PMID:27282391</ref> [[http://www.uniprot.org/uniprot/SPT5H_HUMAN SPT5H_HUMAN]] 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.<ref>PMID:9450929</ref> <ref>PMID:9514752</ref> <ref>PMID:9857195</ref> <ref>PMID:10199401</ref> <ref>PMID:10393184</ref> <ref>PMID:10421630</ref> <ref>PMID:10075709</ref> <ref>PMID:10454543</ref> <ref>PMID:10912001</ref> <ref>PMID:10757782</ref> <ref>PMID:11112772</ref> <ref>PMID:11553615</ref> <ref>PMID:11809800</ref> <ref>PMID:12653964</ref> <ref>PMID:12718890</ref> <ref>PMID:15380072</ref> <ref>PMID:14701750</ref> <ref>PMID:15136722</ref> <ref>PMID:16214896</ref>
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[[http://www.uniprot.org/uniprot/RPB9_PIG RPB9_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). [[http://www.uniprot.org/uniprot/I3LGP4_PIG I3LGP4_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031] [[http://www.uniprot.org/uniprot/SPT4H_HUMAN SPT4H_HUMAN]] 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 [[http://www.uniprot.org/uniprot/NELFD_HUMAN NELFD_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex.<ref>PMID:10199401</ref> <ref>PMID:12612062</ref> [[http://www.uniprot.org/uniprot/I3LCB2_PIG I3LCB2_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.[PIRNR:PIRNR000779] [[http://www.uniprot.org/uniprot/NELFA_HUMAN NELFA_HUMAN]] Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. Probably required to interact with the RNA polymerase II complex.<ref>PMID:10199401</ref> <ref>PMID:12563561</ref> <ref>PMID:12612062</ref> [[http://www.uniprot.org/uniprot/SPT5H_HUMAN SPT5H_HUMAN]] 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.<ref>PMID:9450929</ref> <ref>PMID:9514752</ref> <ref>PMID:9857195</ref> <ref>PMID:10199401</ref> <ref>PMID:10393184</ref> <ref>PMID:10421630</ref> <ref>PMID:10075709</ref> <ref>PMID:10454543</ref> <ref>PMID:10912001</ref> <ref>PMID:10757782</ref> <ref>PMID:11112772</ref> <ref>PMID:11553615</ref> <ref>PMID:11809800</ref> <ref>PMID:12653964</ref> <ref>PMID:12718890</ref> <ref>PMID:15380072</ref> <ref>PMID:14701750</ref> <ref>PMID:15136722</ref> <ref>PMID:16214896</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6gml" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6gml" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Negative elongation factor|Negative elongation factor]]
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*[[RNA polymerase|RNA polymerase]]
== References ==
== References ==
<references/>
<references/>
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[[Category: DNA-directed RNA polymerase]]
[[Category: DNA-directed RNA polymerase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Cramer, P]]
[[Category: Cramer, P]]

Revision as of 18:23, 11 December 2019

Structure of paused transcription complex Pol II-DSIF-NELF

PDB ID 6gml

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