logo

SCIENTIA SINICA Vitae, Volume 49, Issue 9: 1143-1154(2019) https://doi.org/10.1360/SSV-2019-0154

Research progress in structure and function of polymerase-associated factor 1 complex

More info
  • ReceivedJul 25, 2019
  • AcceptedAug 9, 2019
  • PublishedSep 16, 2019

Abstract

Polymerase-associated factor 1 (Paf1) complex is a highly conserved multi-subunit complex in eukaryotes. Yeast Paf1 complex is composed of five subunits (Ctr9, Paf1, Leo1, Cdc73, and Rtf1), but the human Paf1 complex contains an additional subunit Ski8. The Paf1 complex was found to be involved in numerous cellular activities, such as regulating all stages of the RNA polymerase II transcription cycle, processing and nuclear export of nascent transcripts, maintenance of chromatin structure or embryonic stem cell pluripotency, DNA damage and repair, and the occurrence and development of tumors. Here, we review the important research progress of Paf1 complex in recent years from the aspects of structure and function, propose some scientific questions related to Paf1 complex that urgently need to be solved, and prospect for future research directions.


Funded by

国家自然科学基金(31670758,31870750)


References

[1] Zhou Q, Li T, Price D H. RNA polymerase Ⅱ elongation control. Annu Rev Biochem, 2012, 81: 119-143 CrossRef PubMed Google Scholar

[2] Wade P A, Werel W, Fentzke R C, et al. A novel collection of accessory factors associated with yeast RNA polymerase Ⅱ. Protein Expres Purif, 1996, 8: 85-90 CrossRef PubMed Google Scholar

[3] Shi X, Chang M, Wolf A J, et al. Cdc73p and Paf1p are found in a novel RNA polymerase Ⅱ-containing complex distinct from the Srbp-containing holoenzyme. Mol Cell Biol, 1997, 17: 1160-1169 CrossRef PubMed Google Scholar

[4] Tomson B N, Arndt K M. The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states. BBA-Gene Regul Mech, 2013, 1829: 116-126 CrossRef PubMed Google Scholar

[5] Krogan N J, Kim M, Ahn S H, et al. RNA polymerase Ⅱ elongation factors of Saccharomyces cerevisiae: A targeted proteomics approach. Mol Cell Biol, 2002, 22: 6979-6992 CrossRef PubMed Google Scholar

[6] Mueller C L, Jaehning J A. Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase Ⅱ complex. Mol Cell Biol, 2002, 22: 1971-1980 CrossRef PubMed Google Scholar

[7] Squazzo S L, Costa P J, Lindstrom D L, et al. The Paf1 complex physically and functionally associates with transcription elongation factors in vivo. EMBO J, 2002, 21: 1764-1774 CrossRef Google Scholar

[8] Cao Q F, Yamamoto J, Isobe T, et al. Characterization of the human transcription elongation factor Rtf1: Evidence for nonoverlapping functions of Rtf1 and the Paf1 complex. Mol Cell Biol, 2015, 35: 3459-3470 CrossRef PubMed Google Scholar

[9] Chu X, Qin X, Xu H, et al. Structural insights into Paf1 complex assembly and histone binding. Nucleic Acids Res, 2013, 41: 10619-10629 CrossRef PubMed Google Scholar

[10] Krogan N J, Dover J, Wood A, et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation. Mol Cell, 2003, 11: 721-729 CrossRef Google Scholar

[11] Ng H H, Dole S, Struhl K. The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B. J Biol Chem, 2003, 278: 33625-33628 CrossRef PubMed Google Scholar

[12] Wood A, Schneider J, Dover J, et al. The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem, 2003, 278: 34739-34742 CrossRef PubMed Google Scholar

[13] Mueller C L, Porter S E, Hoffman M G, et al. The Paf1 complex has functions independent of actively transcribing RNA polymerase Ⅱ. Mol Cell, 2004, 14: 447-456 CrossRef Google Scholar

[14] Sheldon K E, Mauger D M, Arndt K M. A requirement for the Saccharomyces cerevisiae Paf1 complex in snorna 3′ end formation. Mol Cell, 2005, 20: 225-236 CrossRef PubMed Google Scholar

[15] Rozenblatt-Rosen O, Nagaike T, Francis J M, et al. The tumor suppressor Cdc73 functionally associates with CPSF and CstF 3′ mRNA processing factors. Proc Natl Acad Sci USA, 2009, 106: 755-760 CrossRef PubMed ADS Google Scholar

[16] Kim J, Guermah M, Roeder R G. The human Paf1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS. Cell, 2010, 140: 491-503 CrossRef PubMed Google Scholar

[17] Jaehning J A. The Paf1 complex: Platform or player in RNA polymerase Ⅱ transcription?. BBA-Gene Regul Mech, 2010, 1799: 379-388 CrossRef PubMed Google Scholar

[18] Chen F X, Woodfin A R, Gardini A, et al. Paf1, a molecular regulator of promoter-proximal pausing by RNA polymerase Ⅱ. Cell, 2015, 162: 1003-1015 CrossRef PubMed Google Scholar

[19] Yu M, Yang W, Ni T, et al. RNA polymerase Ⅱ-associated factor 1 regulates the release and phosphorylation of paused RNA polymerase Ⅱ. Science, 2015, 350: 1383-1386 CrossRef PubMed ADS Google Scholar

[20] Sadeghi L, Prasad P, Ekwall K, et al. The Paf1 complex factors Leo1 and Paf1 promote local histone turnover to modulate chromatin states in fission yeast. EMBO Rep, 2015, 16: 1673-1687 CrossRef PubMed Google Scholar

[21] Verrier L, Taglini F, Barrales R R, et al. Global regulation of heterochromatin spreading by Leo1. Open Biol, 2015, 5: 150045 CrossRef PubMed Google Scholar

[22] Yang Y, Li W, Hoque M, et al. Paf complex plays novel subunit-specific roles in alternative cleavage and polyadenylation. PLoS Genet, 2016, 12: e1005794 CrossRef PubMed Google Scholar

[23] Moniaux N, Nemos C, Schmied B M, et al. The human homologue of the RNA polymerase Ⅱ-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis. Oncogene, 2006, 25: 3247-3257 CrossRef PubMed Google Scholar

[24] Hanks S, Perdeaux E R, Seal S, et al. Germline mutations in the Paf1 complex gene CTR9 predispose to wilms tumour. Nat Commun, 2014, 5: 4398 CrossRef PubMed ADS Google Scholar

[25] Carpten J D, Robbins C M, Villablanca A, et al. HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw tumor syndrome. Nat Genet, 2002, 32: 676-680 CrossRef PubMed Google Scholar

[26] de Jong R N, Truffault V, Diercks T, et al. Structure and DNA binding of the human Rtf1 Plus3 domain. Structure, 2008, 16: 149-159 CrossRef PubMed Google Scholar

[27] Wier A D, Mayekar M K, Héroux A, et al. Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin. Proc Natl Acad Sci USA, 2013, 110: 17290-17295 CrossRef PubMed ADS Google Scholar

[28] Van Oss S B, Shirra M K, Bataille A R, et al. The histone modification domain of Paf1 complex subunit Rtf1 directly stimulates H2B ubiquitylation through an interaction with Rad6. Mol Cell, 2016, 64: 815-825 CrossRef PubMed Google Scholar

[29] Amrich C G, Davis C P, Rogal W P, et al. Cdc73 subunit of Paf1 complex contains C-terminal Ras-like domain that promotes association of Paf1 complex with chromatin. J Biol Chem, 2012, 287: 10863-10875 CrossRef PubMed Google Scholar

[30] Sun W, Kuang X L, Liu Y P, et al. Crystal structure of the N-terminal domain of human Cdc73 and its implications for the hyperparathyroidism-jaw tumor (HPT-JT) syndrome. Sci Rep, 2017, 7: 15638 CrossRef PubMed ADS Google Scholar

[31] Xie Y, Zheng M, Chu X, et al. Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation. Nat Commun, 2018, 9: 3795 CrossRef PubMed ADS Google Scholar

[32] Deng P, Zhou Y, Jiang J, et al. Transcriptional elongation factor Paf1 core complex adopts a spirally wrapped solenoidal topology. Proc Natl Acad Sci USA, 2018, 115: 9998-10003 CrossRef PubMed Google Scholar

[33] Xu Y, Bernecky C, Lee C T, et al. Architecture of the RNA polymerase Ⅱ-Paf1C-TFIIS transcription elongation complex. Nat Commun, 2017, 8: 15741 CrossRef PubMed ADS Google Scholar

[34] Vos S M, Farnung L, Boehning M, et al. Structure of activated transcription complex Pol Ⅱ-DSIF-PAF-SPT6. Nature, 2018, 560: 607-612 CrossRef PubMed ADS Google Scholar

[35] KIreeva M, Trang C, Matevosyan G, et al. RNA-DNA and DNA-DNA base-pairing at the upstream edge of the transcription bubble regulate translocation of RNA polymerase and transcription rate. Nucleic Acids Res, 2018, 46: 5764-5775 CrossRef PubMed Google Scholar

[36] Halbach F, Reichelt P, Rode M, et al. The yeast Ski complex: Crystal structure and RNA channeling to the exosome complex. Cell, 2013, 154: 814-826 CrossRef PubMed Google Scholar

[37] Schmidt C, Kowalinski E, Shanmuganathan V, et al. The cryo-EM structure of a ribosome–Ski2-Ski3-Ski8 helicase complex. Science, 2016, 354: 1431-1433 CrossRef PubMed ADS Google Scholar

[38] Pokholok D K, Hannett N M, Young R A. Exchange of RNA polymerase Ⅱ initiation and elongation factors during gene expression in vivo. Mol Cell, 2002, 9: 799-809 CrossRef Google Scholar

[39] Kim M, Ahn S H, Krogan N J, et al. Transitions in RNA polymerase Ⅱ elongation complexes at the 3′ ends of genes. EMBO J, 2004, 23: 354-364 CrossRef PubMed Google Scholar

[40] Laribee R N, Krogan N J, Xiao T, et al. Bur kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the Paf elongation complex. Curr Biol, 2005, 15: 1487-1493 CrossRef PubMed Google Scholar

[41] Qiu H, Hu C, Gaur N A, et al. Pol Ⅱ CTD kinases Bur1 and Kin28 promote Spt5 CTR-independent recruitment of Paf1 complex. EMBO J, 2012, 31: 3494-3505 CrossRef PubMed Google Scholar

[42] Liu Y, Warfield L, Zhang C, et al. Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the Paf complex. Mol Cell Biol, 2009, 29: 4852-4863 CrossRef PubMed Google Scholar

[43] Zhou K, Kuo W H W, Fillingham J, et al. Control of transcriptional elongation and cotranscriptional histone modification by the yeast BUR kinase substrate Spt5. Proc Natl Acad Sci USA, 2009, 106: 6956-6961 CrossRef PubMed ADS Google Scholar

[44] Yamada T, Yamaguchi Y, Inukai N, et al. P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation. Mol Cell, 2006, 21: 227-237 CrossRef PubMed Google Scholar

[45] Mbogning J, Nagy S, Pagé V, et al. The Paf complex and Prf1/Rtf1 delineate distinct Cdk9-dependent pathways regulating transcription elongation in fission yeast. PLoS Genet, 2013, 9: e1004029 CrossRef PubMed Google Scholar

[46] Warner M H, Roinick K L, Arndt K M. Rtf1 is a multifunctional component of the Paf1 complex that regulates gene expression by directing cotranscriptional histone modification. Mol Cell Biol, 2007, 27: 6103-6115 CrossRef PubMed Google Scholar

[47] Mayekar M K, Gardner R G, Arndt K M. The recruitment of the Saccharomyces cerevisiae Paf1 complex to active genes requires a domain of Rtf1 that directly interacts with the Spt4-Spt5 complex. Mol Cell Biol, 2013, 33: 3259-3273 CrossRef PubMed Google Scholar

[48] Piro A S, Mayekar M K, Warner M H, et al. Small region of Rtf1 protein can substitute for complete Paf1 complex in facilitating global histone H2B ubiquitylation in yeast. Proc Natl Acad Sci USA, 2012, 109: 10837-10842 CrossRef PubMed ADS Google Scholar

[49] Dermody J L, Buratowski S. Leo1 subunit of the yeast Paf1 complex binds RNA and contributes to complex recruitment. J Biol Chem, 2010, 285: 33671-33679 CrossRef PubMed Google Scholar

[50] Worden E J, Hoffmann N A, Hicks C W, et al. Mechanism of cross-talk between H2B ubiquitination and H3 methylation by Dot1L. Cell, 2019, 176: 1490-1501.e12 CrossRef PubMed Google Scholar

[51] Kim J, Roeder R G. Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-rad6 interactions mediate histone H2B ubiquitylation in yeast. J Biol Chem, 2009, 284: 20582-20592 CrossRef PubMed Google Scholar

[52] Tomson B N, Davis C P, Warner M H, et al. Identification of a role for histone H2B ubiquitylation in noncoding RNA 3′-end formation through mutational analysis of Rtf1 in Saccharomyces cerevisiae. Genetics, 2011, 188: 273-289 CrossRef PubMed Google Scholar

[53] Dover J, Schneider J, Tawiah-Boateng M A, et al. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J Biol Chem, 2002, 277: 28368-28371 CrossRef PubMed Google Scholar

[54] Nakanishi S, Lee J S, Gardner K E, et al. Histone H2BK123 monoubiquitination is the critical determinant for H3K4 and H3K79 trimethylation by COMPASS and Dot1. J Cell Biol, 2009, 186: 371-377 CrossRef PubMed Google Scholar

[55] Ng H H, Robert F, Young R A, et al. Targeted recruitment of Set1 histone methylase by elongating Pol Ⅱ provides a localized mark and memory of recent transcriptional activity. Mol Cell, 2003, 11: 709-719 CrossRef Google Scholar

[56] Chu Y, Simic R, Warner M H, et al. Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J, 2007, 26: 4646-4656 CrossRef PubMed Google Scholar

[57] Venkatesh S, Workman J L. Set2 mediated H3 lysine 36 methylation: Regulation of transcription elongation and implications in organismal development. WIREs Dev Biol, 2013, 2: 685-700 CrossRef PubMed Google Scholar

[58] Kim J, Guermah M, McGinty R K, et al. Rad6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells. Cell, 2009, 137: 459-471 CrossRef PubMed Google Scholar

[59] Minsky N, Shema E, Field Y, et al. Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells. Nat Cell Biol, 2008, 10: 483-488 CrossRef PubMed Google Scholar

[60] Wu L, Zee B M, Wang Y, et al. The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation. Mol Cell, 2011, 43: 132-144 CrossRef PubMed Google Scholar

[61] Wu L, Li L, Zhou B, et al. H2B ubiquitylation promotes RNA Pol Ⅱ processivity via Paf1 and pTEFb. Mol Cell, 2014, 54: 920-931 CrossRef PubMed Google Scholar

[62] Kowalik K M, Shimada Y, Flury V, et al. The Paf1 complex represses small-RNA-mediated epigenetic gene silencing. Nature, 2015, 520: 248-252 CrossRef PubMed ADS Google Scholar

[63] Rondón A G, Gallardo M, García-Rubio M, et al. Molecular evidence indicating that the yeast PAF complex is required for transcription elongation. EMBO Rep, 2004, 5: 47-53 CrossRef PubMed Google Scholar

[64] Penheiter K L, Washburn T M, Porter S E, et al. A posttranscriptional role for the yeast Paf1-RNA polymerase Ⅱ complex is revealed by identification of primary targets. Mol Cell, 2005, 20: 213-223 CrossRef PubMed Google Scholar

[65] Kwak H, Lis J T. Control of transcriptional elongation. Annu Rev Genet, 2013, 47: 483-508 CrossRef PubMed Google Scholar

[66] Adelman K, Lis J T. Promoter-proximal pausing of RNA polymerase Ⅱ: Emerging roles in metazoans. Nat Rev Genet, 2012, 13: 720-731 CrossRef PubMed Google Scholar

[67] Li J, Gilmour D S. Distinct mechanisms of transcriptional pausing orchestrated by GAGA factor and M1BP, a novel transcription factor. EMBO J, 2013, 32: 1829-1841 CrossRef PubMed Google Scholar

[68] Peterlin B M, Price D H. Controlling the elongation phase of transcription with P-TEFb. Mol Cell, 2006, 23: 297-305 CrossRef PubMed Google Scholar

[69] Liu X, Kraus W L, Bai X. Ready, pause, go: Regulation of RNA polymerase Ⅱ pausing and release by cellular signaling pathways. Trends Biochem Sci, 2015, 40: 516-525 CrossRef PubMed Google Scholar

[70] Farrell A S, Sears R C. Myc degradation. Cold Spring Harbor Perspect Med, 2014, 4: a014365 CrossRef PubMed Google Scholar

[71] McMahon S B, Wood M A, Cole M D. The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol Cell Biol, 2000, 20: 556-562 CrossRef PubMed Google Scholar

[72] Eberhardy S R, Farnham P J. Myc Recruits P-TEFb to mediate the final step in the transcriptional activation of the cad promoter. J Biol Chem, 2002, 277: 40156-40162 CrossRef PubMed Google Scholar

[73] Jaenicke L A, von Eyss B, Carstensen A, et al. Ubiquitin-dependent turnover of MYC antagonizes Myc/Paf1c complex accumulation to drive transcriptional elongation. Mol Cell, 2016, 61: 54-67 CrossRef PubMed Google Scholar

[74] Van Oss S B, Cucinotta C E, Arndt K M. Emerging insights into the roles of the Paf1 complex in gene regulation. Trends Biochem Sci, 2017, 42: 788-798 CrossRef PubMed Google Scholar

[75] Bartkowiak B, Liu P, Phatnani H P, et al. CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1. Genes Dev, 2010, 24: 2303-2316 CrossRef PubMed Google Scholar

[76] Lu X, Zhu X, Li Y, et al. Multiple P-TEFBs cooperatively regulate the release of promoter-proximally paused RNA polymerase Ⅱ. Nucleic Acids Res, 2016, 44: 6853-6867 CrossRef PubMed Google Scholar

[77] Nordick K, Hoffman M G, Betz J L, et al. Direct interactions between the Paf1 complex and a cleavage and polyadenylation factor are revealed by dissociation of Paf1 from RNA polymerase Ⅱ. Eukaryot Cell, 2008, 7: 1158-1167 CrossRef PubMed Google Scholar

[78] Ahn S H, Kim M, Buratowski S. Phosphorylation of serine 2 within the RNA polymerase Ⅱ C-terminal domain couples transcription and 3′ end processing. Mol Cell, 2004, 13: 67-76 CrossRef Google Scholar

[79] Licatalosi D D, Geiger G, Minet M, et al. Functional interaction of yeast pre-mRNA 3′ end processing factors with RNA polymerase Ⅱ. Mol Cell, 2002, 9: 1101-1111 CrossRef Google Scholar

[80] Fischl H, Howe F S, Furger A, et al. Paf1 has distinct roles in transcription elongation and differential transcript fate. Mol Cell, 2017, 65: 685-698.e8 CrossRef PubMed Google Scholar

[81] Wysocki R, Javaheri A, Allard S, et al. Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol Cell Biol, 2005, 25: 8430-8443 CrossRef PubMed Google Scholar

[82] Huyen Y, Zgheib O, DiTullio Jr. R A, et al. Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature, 2004, 432: 406-411 CrossRef PubMed ADS Google Scholar

[83] Nakamura K, Kato A, Kobayashi J, et al. Regulation of homologous recombination by RNF20-dependent H2B ubiquitination. Mol Cell, 2011, 41: 515-528 CrossRef PubMed Google Scholar

[84] Herr P, Lundin C, Evers B, et al. A genome-wide IR-induced Rad51 foci RNAi screen identifies Cdc73 involved in chromatin remodeling for DNA repair. Cell Discov, 2015, 1: 15034 CrossRef PubMed Google Scholar

[85] Landsverk H B, Sandquist L E, Sridhara S C, et al. Regulation of ATR activity via the RNA polymerase Ⅱ associated factors Cdc73 and PNUTS-PP1. Nucleic Acids Res, 2019, 47: 1797-1813 CrossRef PubMed Google Scholar

[86] Ding L, Paszkowski-Rogacz M, Nitzsche A, et al. A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1 complex for embryonic stem cell identity. Cell Stem Cell, 2009, 4: 403-415 CrossRef PubMed Google Scholar

[87] Ponnusamy M P, Deb S, Dey P, et al. RNA polymerase Ⅱ-association factor 1 (Paf1/PD2) maintains self-renewal by its interaction with Oct3/4 in mouse embryonic stem cells. Stem Cells, 2009, : doi: 10.1002/stem.237 CrossRef PubMed Google Scholar

[88] Karmakar S, Seshacharyulu P, Lakshmanan I, et al. Hpaf1/PD2 interacts with Oct3/4 to promote self-renewal of ovarian cancer stem cells. Oncotarget, 2017, 8: 14806-14820 CrossRef PubMed Google Scholar

[89] Bahrampour S, Thor S. Ctr9, a key component of the Paf1 complex, affects proliferation and terminal differentiation in the developing Drosophila nervous system. G3, 2016, 6: 3229-3239 CrossRef PubMed Google Scholar

[90] Nguyen C T, Langenbacher A, Hsieh M, et al. The Paf1 complex component Leo1 is essential for cardiac and neural crest development in zebrafish. Dev Biol, 2010, 341: 167-175 CrossRef PubMed Google Scholar

[91] Strikoudis A, Lazaris C, Ntziachristos P, et al. Opposing functions of H2BK120 ubiquitylation and H3k79 methylation in the regulation of pluripotency by the Paf1 complex. Cell Cycle, 2017, 16: 2315-2322 CrossRef PubMed Google Scholar

[92] Strikoudis A, Lazaris C, Trimarchi T, et al. Regulation of transcriptional elongation in pluripotency and cell differentiation by the PHD-finger protein Phf5a. Nat Cell Biol, 2016, 18: 1127-1138 CrossRef PubMed Google Scholar

[93] Zeng H, Xu W. Ctr9, a key subunit of PAFc, affects global estrogen signaling and drives ERα-positive breast tumorigenesis. Genes Dev, 2015, 29: 2153-2167 CrossRef PubMed Google Scholar

[94] Zhi X, Giroux-Leprieur E, Wislez M, et al. Human RNA polymerase Ⅱ associated factor 1 complex promotes tumorigenesis by activating c-Myc transcription in non-small cell lung cancer. Biochem Biophys Res Commun, 2015, 465: 685-690 CrossRef PubMed Google Scholar

[95] Karmakar S, Dey P, Vaz A P, et al. Pd2/Paf1 at the crossroads of the cancer network. Cancer Res, 2018, 78: 313-319 CrossRef PubMed Google Scholar

  • Figure 1

    Structures of subunit or subcomplex of Paf1 complex. A: Rtf1-Plus3 domain (Homo sapiens, PDB: 2BZE). B: Rtf1-Spt5 subcomplex (Homo sapiens, PDB: 4L1U). C: Rtf1-HMD domain (Saccharomyces cerevisiae, PDB: 5E8B). D: Cdc73 C-terminal domain (Saccharomyces cerevisiae, PDB: 3V46). E: Cdc73 N-Terminal domain (Homo sapiens, PDB: 5YDE). F: Paf1-Leo1 subcomplex (Homo sapiens, PDB: 4M6T). G: Ctr9-Paf1 subcomplex (Saccharomyces cerevisiae, PDB: 5ZYP). H: Ctr9-Paf1 subcomplex (Homo sapiens, 5ZYQ). I: Ctr9-Paf1-Cdc73 subcomplex (Myceliophthora thermophila, PDB: 6AF0). J: Pol Ⅱ-DSIF-PAF-SPT6 (Homo sapiens and Sus scrofa, PDB: 6GMH)

Copyright 2019 Science China Press Co., Ltd. 《中国科学》杂志社有限责任公司 版权所有

京ICP备18024590号-1