Log in

Relevant bibliographies by topics / RNA polymerase II C-terminal domain / Journal articles

To see the other types of publications on this topic, follow the link: RNA polymerase II C-terminal domain.

Journal articles on the topic 'RNA polymerase II C-terminal domain'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'RNA polymerase II C-terminal domain.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Dubois, Marie-Françoise, François Bonnet, Céline Cass, Van Trung Nguyen, Benoit Palancade, and Olivier Bensaude. "Modulation of RNA polymerase II C-terminal domain phosphorylation." Biochemistry and Cell Biology 77, no. 4 (1999): 392–93. http://dx.doi.org/10.1139/o99-903i.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Stiller, J. W., and B. D. Hall. "Evolution of the RNA polymerase II C-terminal domain." Proceedings of the National Academy of Sciences 99, no. 9 (2002): 6091–96. http://dx.doi.org/10.1073/pnas.082646199.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Abbas, Ata, Todd Romigh, and Charis Eng. "PTEN interacts with RNA polymerase II to dephosphorylate polymerase II C-terminal domain." Oncotarget 10, no. 48 (2019): 4951–59. http://dx.doi.org/10.18632/oncotarget.27128.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Dahmus, Michael E. "Phosphorylation of the C-terminal domain of RNA polymerase II." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1261, no. 2 (1995): 171–82. http://dx.doi.org/10.1016/0167-4781(94)00233-s.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Sano, Motoaki, Manabu Shirai, Derrick J. Rossi, et al. "RNA polymerase II C-terminal domain kinases in heart failure." Journal of Cardiac Failure 9, no. 5 (2003): S4. http://dx.doi.org/10.1016/s1071-9164(03)00165-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

García, Alicia, Emanuel Rosonina, James L. Manley, and Olga Calvo. "Sub1 Globally Regulates RNA Polymerase II C-Terminal Domain Phosphorylation." Molecular and Cellular Biology 30, no. 21 (2010): 5180–93. http://dx.doi.org/10.1128/mcb.00819-10.

Full text

Abstract:

ABSTRACT The transcriptional coactivator Sub1 has been implicated in several aspects of mRNA metabolism in yeast, such as activation of transcription, termination, and 3′-end formation. Here, we present evidence that Sub1 plays a significant role in controlling phosphorylation of the RNA polymerase II large subunit C-terminal domain (CTD). We show that SUB1 genetically interacts with the genes encoding all four known CTD kinases, SRB10, KIN28, BUR1, and CTK1, suggesting that Sub1 acts to influence CTD phosphorylation at more than one step of the transcription cycle. To address this directly, w

APA, Harvard, Vancouver, ISO, and other styles

7

Bensaude, Olivier, François Bonnet, Céline Cassé, Marie-Françoise Dubois, Van Trung Nguyen, and Benoit Palancade. "Regulated phosphorylation of the RNA polymerase II C-terminal domain (CTD)." Biochemistry and Cell Biology 77, no. 4 (1999): 249–55. http://dx.doi.org/10.1139/o99-047.

Full text

Abstract:

The largest subunit of RNA polymerase II has an intriguing feature in its carboxyl-terminal domain (CTD) that consists of multiple repeats of an evolutionary conserved motif of seven amino acids. CTD phosphorylation plays a pivotal role in controlling mRNA synthesis and maturation. In exponentially growing cells, the phosphate turnover on the CTD is fast; it is blocked by common inhibitors of transcription, such as 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and actinomycin D. Transcription-independent changes in CTD phosphorylation are observed at critical developmental stages, such as m

APA, Harvard, Vancouver, ISO, and other styles

8

Dahmus, Michael E. "Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II." Journal of Biological Chemistry 271, no. 32 (1996): 19009–12. http://dx.doi.org/10.1074/jbc.271.32.19009.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

O'Brien, Thomas, Steven Hardin, Arno Greenleaf, and John T. Lis. "Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation." Nature 370, no. 6484 (1994): 75–77. http://dx.doi.org/10.1038/370075a0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Gerber, Hans-Peter, Michael Hagmann, Katja Seipel, et al. "RNA polymerase II C-terminal domain required for enhancer-driven transcription." Nature 374, no. 6523 (1995): 660–62. http://dx.doi.org/10.1038/374660a0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Patturajan, Meera, Xiangyun Wei, Ronald Berezney, and Jeffry L. Corden. "A Nuclear Matrix Protein Interacts with the Phosphorylated C-Terminal Domain of RNA Polymerase II." Molecular and Cellular Biology 18, no. 4 (1998): 2406–15. http://dx.doi.org/10.1128/mcb.18.4.2406.

Full text

Abstract:

ABSTRACT Yeast two-hybrid screening has led to the identification of a family of proteins that interact with the repetitive C-terminal repeat domain (CTD) of RNA polymerase II (A. Yuryev et al., Proc. Natl. Acad. Sci. USA 93:6975–6980, 1996). In addition to serine/arginine-rich SR motifs, the SCAFs (SR-like CTD-associated factors) contain discrete CTD-interacting domains. In this paper, we show that the CTD-interacting domain of SCAF8 specifically binds CTD molecules phosphorylated on serines 2 and 5 of the consensus sequence Tyr1Ser2Pro3Thr4Ser5Pro6Ser7. In addition, we demonstrate that SCAF8

APA, Harvard, Vancouver, ISO, and other styles

12

Jones, Janice C., Hemali P. Phatnani, Timothy A. Haystead, Justin A. MacDonald, S. Munir Alam, and Arno L. Greenleaf. "C-terminal Repeat Domain Kinase I Phosphorylates Ser2 and Ser5 of RNA Polymerase II C-terminal Domain Repeats." Journal of Biological Chemistry 279, no. 24 (2004): 24957–64. http://dx.doi.org/10.1074/jbc.m402218200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Corden, Jeffry L. "RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template." Chemical Reviews 113, no. 11 (2013): 8423–55. http://dx.doi.org/10.1021/cr400158h.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Sharma, Priyanka, Antonios Lioutas, Narcis Fernandez-Fuentes, et al. "Arginine Citrullination at the C-Terminal Domain Controls RNA Polymerase II Transcription." Molecular Cell 73, no. 1 (2019): 84–96. http://dx.doi.org/10.1016/j.molcel.2018.10.016.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Simonti, Corinne N., Katherine S. Pollard, Sebastian Schröder, et al. "Evolution of lysine acetylation in the RNA polymerase II C-terminal domain." BMC Evolutionary Biology 15, no. 1 (2015): 35. http://dx.doi.org/10.1186/s12862-015-0327-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Meredith, Gavin D., Wei-Hau Chang, Yang Li, David A. Bushnell, Seth A. Darst, and Roger D. Kornberg. "The C-terminal Domain Revealed in the Structure of RNA Polymerase II." Journal of Molecular Biology 258, no. 3 (1996): 413–19. http://dx.doi.org/10.1006/jmbi.1996.0258.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Washington, Kareem, Tatyana Ammosova, Monique Beullens, et al. "Protein Phosphatase-1 Dephosphorylates the C-terminal Domain of RNA Polymerase-II." Journal of Biological Chemistry 277, no. 43 (2002): 40442–48. http://dx.doi.org/10.1074/jbc.m205687200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Devaiah, Ballachanda N., and Dinah S. Singer. "Cross-talk Among RNA Polymerase II Kinases Modulates C-terminal Domain Phosphorylation." Journal of Biological Chemistry 287, no. 46 (2012): 38755–66. http://dx.doi.org/10.1074/jbc.m112.412015.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Harikrishna, Reddy R., Hackyoung Kim, Kwangmo Noh, and Young Jun Kim. "The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1." BMB Reports 47, no. 4 (2014): 192–96. http://dx.doi.org/10.5483/bmbrep.2014.47.4.060.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Kang, Chang Ho, Yue Feng, Meenu Vikram, et al. "Arabidopsis thaliana PRP40s are RNA polymerase II C-terminal domain-associating proteins." Archives of Biochemistry and Biophysics 484, no. 1 (2009): 30–38. http://dx.doi.org/10.1016/j.abb.2009.01.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Moisan, Annie, Chantal Larochelle, Benoît Guillemette, and Luc Gaudreau. "BRCA1 Can Modulate RNA Polymerase II Carboxy-Terminal Domain Phosphorylation Levels." Molecular and Cellular Biology 24, no. 16 (2004): 6947–56. http://dx.doi.org/10.1128/mcb.24.16.6947-6956.2004.

Full text

Abstract:

ABSTRACT A high incidence of breast and ovarian cancers has been linked to mutations in the BRCA1 gene. BRCA1 has been shown to be involved in both positive and negative regulation of gene activity as well as in numerous other processes such as DNA repair and cell cycle regulation. Since modulation of the RNA polymerase II carboxy-terminal domain (CTD) phosphorylation levels could constitute an interface to all these functions, we wanted to directly test the possibility that BRCA1 might regulate the phosphorylation state of the CTD. We have shown that the BRCA1 C-terminal region can negatively

APA, Harvard, Vancouver, ISO, and other styles

22

Engelhardt, Othmar G., Matt Smith, and Ervin Fodor. "Association of the Influenza A Virus RNA-Dependent RNA Polymerase with Cellular RNA Polymerase II." Journal of Virology 79, no. 9 (2005): 5812–18. http://dx.doi.org/10.1128/jvi.79.9.5812-5818.2005.

Full text

Abstract:

ABSTRACT Transcription by the influenza virus RNA-dependent RNA polymerase is dependent on cellular RNA processing activities that are known to be associated with cellular RNA polymerase II (Pol II) transcription, namely, capping and splicing. Therefore, it had been hypothesized that transcription by the viral RNA polymerase and Pol II might be functionally linked. Here, we demonstrate for the first time that the influenza virus RNA polymerase complex interacts with the large subunit of Pol II via its C-terminal domain. The viral polymerase binds hyperphosphorylated forms of Pol II, indicating

APA, Harvard, Vancouver, ISO, and other styles

23

Aitken, Stuart, Ross D. Alexander, and Jean D. Beggs. "A rule-based kinetic model of RNA polymerase II C-terminal domain phosphorylation." Journal of The Royal Society Interface 10, no. 86 (2013): 20130438. http://dx.doi.org/10.1098/rsif.2013.0438.

Full text

Abstract:

The complexity of many RNA processing pathways is such that a conventional systems modelling approach is inadequate to represent all the molecular species involved. We demonstrate that rule-based modelling permits a detailed model of a complex RNA signalling pathway to be defined. Phosphorylation of the RNA polymerase II (RNAPII) C-terminal domain (CTD; a flexible tail-like extension of the largest subunit) couples pre-messenger RNA capping, splicing and 3′ end maturation to transcriptional elongation and termination, and plays a central role in integrating these processes. The phosphorylation

APA, Harvard, Vancouver, ISO, and other styles

24

Baskaran, R., M. E. Dahmus, and J. Y. Wang. "Tyrosine phosphorylation of mammalian RNA polymerase II carboxyl-terminal domain." Proceedings of the National Academy of Sciences 90, no. 23 (1993): 11167–71. http://dx.doi.org/10.1073/pnas.90.23.11167.

Full text

Abstract:

The carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II is composed of tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser. Phosphorylation of the CTD occurs during formation of the initiation complex and is correlated with the transition from complex assembly to elongation. Previously, serine and threonine residues within the CTD have been shown to be modified by the addition of phosphate and by the addition of O-linked GlcNAc. Our results establish that the CTD is also modified in vivo by phosphorylation on tyrosine. Furthermore, a nuclear tyrosine kin

APA, Harvard, Vancouver, ISO, and other styles

25

Ivanov, Dmitri, Youn Tae Kwak, Jun Guo, and Richard B. Gaynor. "Domains in the SPT5 Protein That Modulate Its Transcriptional Regulatory Properties." Molecular and Cellular Biology 20, no. 9 (2000): 2970–83. http://dx.doi.org/10.1128/mcb.20.9.2970-2983.2000.

Full text

Abstract:

ABSTRACT SPT5 and its binding partner SPT4 regulate transcriptional elongation by RNA polymerase II. SPT4 and SPT5 are involved in both 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole (DRB)-mediated transcriptional inhibition and the activation of transcriptional elongation by the human immunodeficiency virus type 1 (HIV-1) Tat protein. Recent data suggest that P-TEFb, which is composed of CDK9 and cyclin T1, is also critical in regulating transcriptional elongation by SPT4 and SPT5. In this study, we analyze the domains of SPT5 that regulate transcriptional elongation in the presence of either

APA, Harvard, Vancouver, ISO, and other styles

26

Eick, Dirk, and Matthias Geyer. "The RNA Polymerase II Carboxy-Terminal Domain (CTD) Code." Chemical Reviews 113, no. 11 (2013): 8456–90. http://dx.doi.org/10.1021/cr400071f.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Cho, Eun-Jung. "RNA polymerase II carboxy-terminal domain with multiple connections." Experimental & Molecular Medicine 39, no. 3 (2007): 247–54. http://dx.doi.org/10.1038/emm.2007.28.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Palancade, Beno��t, and Olivier Bensaude. "Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation." European Journal of Biochemistry 270, no. 19 (2003): 3859–70. http://dx.doi.org/10.1046/j.1432-1033.2003.03794.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Stiller, John W., and Matthew S. Cook. "Functional Unit of the RNA Polymerase II C-Terminal Domain Lies within Heptapeptide Pairs." Eukaryotic Cell 3, no. 3 (2004): 735–40. http://dx.doi.org/10.1128/ec.3.3.735-740.2004.

Full text

Abstract:

ABSTRACT Unlike all other RNA polymerases, the largest subunit (RPB1) of eukaryotic DNA-dependent RNA polymerase II (RNAP II) has a C-terminal domain (CTD) comprising tandemly repeated heptapeptides with the consensus sequence Y-S-P-T-S-P-S. The tandem structure, heptad consensus, and most key functions of the CTD are conserved between yeast and mammals. In fact, all metazoans, fungi, and green plants examined to date, as well as the nearest protistan relatives of these multicellular groups, contain a tandemly repeated CTD. In contrast, the RNAP II largest subunits from many other eukaryotic o

APA, Harvard, Vancouver, ISO, and other styles

30

Stump, Aram D., and Khrystyna Ostrozhynska. "Selective constraint and the evolution of the RNA Polymerase II C-Terminal Domain." Transcription 4, no. 2 (2013): 77–86. http://dx.doi.org/10.4161/trns.23305.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Suh, Hyunsuk, Dane Z. Hazelbaker, Luis M. Soares, and Stephen Buratowski. "The C-Terminal Domain of Rpb1 Functions on Other RNA Polymerase II Subunits." Molecular Cell 51, no. 6 (2013): 850–58. http://dx.doi.org/10.1016/j.molcel.2013.08.015.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Qian, Hui, Chaoneng Ji, Shuo Zhao, et al. "Expression and characterization of HSPC129, a RNA polymerase II C-terminal domain phosphatase." Molecular and Cellular Biochemistry 303, no. 1-2 (2007): 183–88. http://dx.doi.org/10.1007/s11010-007-9472-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Zhang, Yan, Youngjun Kim, Nicolas Genoud, et al. "Determinants for Dephosphorylation of the RNA Polymerase II C-Terminal Domain by Scp1." Molecular Cell 24, no. 5 (2006): 759–70. http://dx.doi.org/10.1016/j.molcel.2006.10.027.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Gudipati, Rajani Kanth, Tommaso Villa, Jocelyne Boulay, and Domenico Libri. "Phosphorylation of the RNA polymerase II C-terminal domain dictates transcription termination choice." Nature Structural & Molecular Biology 15, no. 8 (2008): 786–94. http://dx.doi.org/10.1038/nsmb.1460.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

de la Mata, Manuel, and Alberto R. Kornblihtt. "RNA polymerase II C-terminal domain mediates regulation of alternative splicing by SRp20." Nature Structural & Molecular Biology 13, no. 11 (2006): 973–80. http://dx.doi.org/10.1038/nsmb1155.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

McCracken, Susan, Nova Fong, Krassimir Yankulov, et al. "The C-terminal domain of RNA polymerase II couples mRNA processing to transcription." Nature 385, no. 6614 (1997): 357–61. http://dx.doi.org/10.1038/385357a0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Feng, Yue, Jae Sook Kang, Sewon Kim, et al. "Arabidopsis SCP1-like small phosphatases differentially dephosphorylate RNA polymerase II C-terminal domain." Biochemical and Biophysical Research Communications 397, no. 2 (2010): 355–60. http://dx.doi.org/10.1016/j.bbrc.2010.05.130.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Zheng, Huarui, Chaoneng Ji, Shaohua Gu, et al. "Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase." Biochemical and Biophysical Research Communications 331, no. 4 (2005): 1401–7. http://dx.doi.org/10.1016/j.bbrc.2005.04.065.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Rodríguez, Carlos F., and Oscar Llorca. "RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes." Cells 9, no. 5 (2020): 1139. http://dx.doi.org/10.3390/cells9051139.

Full text

Abstract:

The Rvb1-Rvb2-Tah1-Pih1 (R2TP) complex is a co-chaperone complex that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II (Pol II) and complexes of the phosphatidylinositol-3-kinase-like family of kinases (PIKKs), such as mTORC1 and ATR/ATRIP. R2TP is made of four subunits: RuvB-like protein 1 (RUVBL1) and RuvB-like 2 (RUVBL2) AAA-type ATPases, RNA polymerase II-associated protein 3 (RPAP3), and the Protein interacting with Hsp90 1 (PIH1) domain-containing protein 1 (PIH1D1). R2TP associates with other proteins as part of a

APA, Harvard, Vancouver, ISO, and other styles

40

Allison, L. A., J. K. Wong, V. D. Fitzpatrick, M. Moyle, and C. J. Ingles. "The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function." Molecular and Cellular Biology 8, no. 1 (1988): 321–29. http://dx.doi.org/10.1128/mcb.8.1.321.

Full text

Abstract:

Using DNA encoding the largest subunit of Drosophila melanogaster RNA polymerase II, we isolated the homologous hamster RPO21 gene. Nucleotide sequencing of both the hamster and D. melanogaster RPO21 DNAs confirmed that the RPO21 polypeptides of these two species, like the Saccharomyces cerevisiae RPO21 polypeptide, contain both an N-terminal region homologous to the Escherichia coli RNA polymerase subunit beta' and a unique polymerase II-specific C-terminal domain. This C-terminal domain, encoded by separate exons in the D. melanogaster and hamster genes, consists of a tandemly repeated hepta

APA, Harvard, Vancouver, ISO, and other styles

41

Allison, L. A., J. K. Wong, V. D. Fitzpatrick, M. Moyle, and C. J. Ingles. "The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function." Molecular and Cellular Biology 8, no. 1 (1988): 321–29. http://dx.doi.org/10.1128/mcb.8.1.321-329.1988.

Full text

Abstract:

Using DNA encoding the largest subunit of Drosophila melanogaster RNA polymerase II, we isolated the homologous hamster RPO21 gene. Nucleotide sequencing of both the hamster and D. melanogaster RPO21 DNAs confirmed that the RPO21 polypeptides of these two species, like the Saccharomyces cerevisiae RPO21 polypeptide, contain both an N-terminal region homologous to the Escherichia coli RNA polymerase subunit beta' and a unique polymerase II-specific C-terminal domain. This C-terminal domain, encoded by separate exons in the D. melanogaster and hamster genes, consists of a tandemly repeated hepta

APA, Harvard, Vancouver, ISO, and other styles

42

Reyes-Reyes, Mariela, and Michael Hampsey. "Role for the Ssu72 C-Terminal Domain Phosphatase in RNA Polymerase II Transcription Elongation." Molecular and Cellular Biology 27, no. 3 (2006): 926–36. http://dx.doi.org/10.1128/mcb.01361-06.

Full text

Abstract:

ABSTRACT The RNA polymerase II (RNAP II) transcription cycle is accompanied by changes in the phosphorylation status of the C-terminal domain (CTD), a reiterated heptapeptide sequence (Y1S2P3T4S5P6S7) present at the C terminus of the largest RNAP II subunit. One of the enzymes involved in this process is Ssu72, a CTD phosphatase with specificity for serine-5-P. Here we report that the ssu72-2-encoded Ssu72-R129A protein is catalytically impaired in vitro and that the ssu72-2 mutant accumulates the serine-5-P form of RNAP II in vivo. An in vitro transcription system derived from the ssu72-2 mut

APA, Harvard, Vancouver, ISO, and other styles

43

Gerber, Mark A., Ali Shilatifard, and Joel C. Eissenberg. "Mutational Analysis of an RNA Polymerase II Elongation Factor in Drosophila melanogaster." Molecular and Cellular Biology 25, no. 17 (2005): 7803–11. http://dx.doi.org/10.1128/mcb.25.17.7803-7811.2005.

Full text

Abstract:

ABSTRACT The ELL family of proteins function in vitro as elongation factors for RNA polymerase II. Deletion studies have defined domains in mammalian ELL required for transcription elongation activity and RNA polymerase binding in vitro, for transformation of cultured cells when overexpressed, and for leukemogenesis and cell proliferation as part of a leukemic fusion protein. The goal of this study was to identify domains required for chromosome targeting and viability in the unique Drosophila ELL (dELL) protein. Here, we show that an N-terminal domain of dELL is necessary and sufficient for t

APA, Harvard, Vancouver, ISO, and other styles

44

Lee, Jeong-Heon, and David G. Skalnik. "Wdr82 Is a C-Terminal Domain-Binding Protein That Recruits the Setd1A Histone H3-Lys4 Methyltransferase Complex to Transcription Start Sites of Transcribed Human Genes." Molecular and Cellular Biology 28, no. 2 (2007): 609–18. http://dx.doi.org/10.1128/mcb.01356-07.

Full text

Abstract:

ABSTRACT Histone H3-Lys4 trimethylation is associated with the transcription start site of transcribed genes, but the molecular mechanisms that control this distribution in mammals are unclear. The human Setd1A histone H3-Lys4 methyltransferase complex was found to physically associate with the RNA polymerase II large subunit. The Wdr82 component of the Setd1A complex interacts with the RNA recognition motif of Setd1A and additionally binds to the Ser5-phosphorylated C-terminal domain of RNA polymerase II, which is involved in initiation of transcription, but does not bind to an unphosphorylat

APA, Harvard, Vancouver, ISO, and other styles

45

Rallabandi, Harikrishna Reddy, Palanivel Ganesan, and Young Jun Kim. "Targeting the C-Terminal Domain Small Phosphatase 1." Life 10, no. 5 (2020): 57. http://dx.doi.org/10.3390/life10050057.

Full text

Abstract:

The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1’s major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II CTD). It is also implicated in various pivotal biological activities, such as acting as a driving factor in repressor element 1 (RE-1)-silencing transcription factor (REST) complex, which silences the neuronal genes in non-neuronal cells, G1/S phase transition, and osteoblast differentiation. Recent

APA, Harvard, Vancouver, ISO, and other styles

46

Lei, Lei, Delin Ren, Ann Finkelstein, and Zachary F. Burton. "Functions of the N- and C-Terminal Domains of Human RAP74 in Transcriptional Initiation, Elongation, and Recycling of RNA Polymerase II." Molecular and Cellular Biology 18, no. 4 (1998): 2130–42. http://dx.doi.org/10.1128/mcb.18.4.2130.

Full text

Abstract:

ABSTRACT Transcription factor IIF (TFIIF) cooperates with RNA polymerase II (pol II) during multiple stages of the transcription cycle including preinitiation complex assembly, initiation, elongation, and possibly termination and recycling. Human TFIIF appears to be an α2β2 heterotetramer of RNA polymerase II-associating protein 74- and 30-kDa subunits (RAP74 and RAP30). From inspection of its 517-amino-acid (aa) sequence, the RAP74 subunit appears to comprise separate N- and C-terminal domains connected by a flexible loop. In this study, we present functional data that strongly support this m

APA, Harvard, Vancouver, ISO, and other styles

47

Egloff, Sylvain, and Shona Murphy. "Role of the C-terminal domain of RNA polymerase II in expression of small nuclear RNA genes." Biochemical Society Transactions 36, no. 3 (2008): 537–39. http://dx.doi.org/10.1042/bst0360537.

Full text

Abstract:

Pol II (RNA polymerase II) transcribes the genes encoding proteins and non-coding snRNAs (small nuclear RNAs). The largest subunit of Pol II contains a distinctive CTD (C-terminal domain) comprising a repetitive heptad amino acid sequence, Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. This domain is now known to play a major role in the processes of transcription and co-transcriptional RNA processing in expression of both snRNA and protein-coding genes. The heptapeptide repeat unit can be extensively modified in vivo and covalent modifications of the CTD during the transcription cycle result in the orde

APA, Harvard, Vancouver, ISO, and other styles

48

Yankulov, K., I. Todorov, P. Romanowski, et al. "MCM Proteins Are Associated with RNA Polymerase II Holoenzyme." Molecular and Cellular Biology 19, no. 9 (1999): 6154–63. http://dx.doi.org/10.1128/mcb.19.9.6154.

Full text

Abstract:

ABSTRACT MCMs are a family of proteins related to ATP-dependent helicases that bind to origin recognition complexes and are required for initiation of DNA replication. We report that antibodies against MCM2(BM28) specifically inhibited transcription by RNA polymerase II (Pol II) in microinjected Xenopus oocytes. Consistent with this observation, MCM2 and other MCMs copurified with Pol II and general transcription factors (GTFs) in high-molecular-weight holoenzyme complexes isolated from Xenopus oocytes and HeLa cells. Pol II and GTFs also copurified with MCMs isolated by anti-MCM3 immunoaffini

APA, Harvard, Vancouver, ISO, and other styles

49

Jeronimo, Célia, Alain R. Bataille, and François Robert. "The Writers, Readers, and Functions of the RNA Polymerase II C-Terminal Domain Code." Chemical Reviews 113, no. 11 (2013): 8491–522. http://dx.doi.org/10.1021/cr4001397.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Janke, Abigail M., Da Hee Seo, Vahid Rahmanian, et al. "Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment." Biochemistry 57, no. 17 (2017): 2549–63. http://dx.doi.org/10.1021/acs.biochem.7b00310.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!