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Roger D. Kornberg - One of the best experts on this subject based on the ideXlab platform.
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IDENTIFICATION OF NEW MEDIATOR SUBUNITS IN THE RNA POLYMERASE II HOLOENZYME FROM SACCHAROMYCES CEREVISIAE
The Journal of biological chemistry, 1998Co-Authors: Claes M. Gustafsson, Jenny Beve, Henrik Spåhr, Mary Lui, Hediye Erdjument-bromage, Paul Tempst, Lawrence C. Myers, Roger D. KornbergAbstract:Abstract Mediator was isolated from yeast on the basis of its requirement for transcriptional activation in a fully defined system. We have now identified three new members of mediator in the low molecular mass range by peptide sequence determination. These are the products of the NUT2, CSE2, and MED11 genes. The product of the NUT1 gene is evidently a component of mediator as well. NUT1 and NUT2 were earlier identified as negative regulators of the HO promoter, whereas mutations in CSE2 affect chromosome segregation.MED11 is a previously uncharacterized gene. The existence of these proteins in the mediator complex was verified by Copurification and co-immunoprecipitation with RNA polymerase II holoenzyme.
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Identification of New Mediator Subunits in the RNA Polymerase II Holoenzyme from
1998Co-Authors: Claes M. Gustafsson, Roger D. Kornberg, Jenny Beve, Henrik Spåhr, Mary Lui, Hediye Erdjument-bromage, Paul Tempst, Memorial SloanAbstract:Mediator was isolated from yeast on the basis of its requirement for transcriptional activation in a fully defined system. We have now identified three new members of mediator in the low molecular mass range by peptide sequence determination. These are the products of the NUT2, CSE2, and MED11 genes. The product of the NUT1 gene is evidently a component of mediator as well. NUT1 and NUT2 were earlier identified as negative regulators of the HO promoter, whereas mutations in CSE2 affect chromosome segregation. MED11 is a previously uncharacterized gene. The existence of these proteins in the mediator complex was verified by Copurification and co-immunoprecipitation with RNA polymerase II holoenzyme.
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Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK
Cell, 1994Co-Authors: William J. Feaver, Jesper Q. Svejstrup, N. Lynn Henry, Roger D. KornbergAbstract:Abstract KIN28, a member of the p34 cdc2/CDC28 family of protein kinases, is identified as a subunit of yeast RNA polymerase transcription factor IIH (TFIIH) on the basis of sequence determination, immunological reactivity, and Copurification. KIN28 is, moreover, one of three subunits of TFIIK, a subassembly of TFIIH with protein kinase activity directed toward the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II. Itself a phosphoprotein, KIN28 interacts specifically with the two largest subunits of RNA polymerase II. Previous work of others points to two further associations: KIN28 interacts in vivo with the cyclin CCL1, and KIN28 and CCL1 are homologous to human MO15 and cyclin H, which form the cyclin-dependent kinaseactivating kinase (CAK). We show that human CAK possesses the CTD kinase activity characteristic of TFIIH.
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A multisubunit complex containing the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated from yeast.
Proceedings of the National Academy of Sciences of the United States of America, 1994Co-Authors: Bradley R. Cairns, Young-joon Kim, Michael H. Sayre, Brehon C. Laurent, Roger D. KornbergAbstract:Abstract A complex containing the products of the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 genes and four additional polypeptides has been purified from extracts of the yeast Saccharomyces cerevisiae. Physical association of these proteins was demonstrated by Copurification and coimmunoprecipitation. A potent DNA-dependent ATPase copurified with the complex, and this activity was evidently associated with SWI2/SNF2.
Hiroshi Handa - One of the best experts on this subject based on the ideXlab platform.
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Copurification of Casein Kinase II with Transcription Factor ATF/E4TF3
Nucleic acids research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.
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Copurification of casein kinase ii with transcription factor atf e4tf3
Nucleic Acids Research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.
Tadashi Wada - One of the best experts on this subject based on the ideXlab platform.
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Copurification of Casein Kinase II with Transcription Factor ATF/E4TF3
Nucleic acids research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.
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Copurification of casein kinase ii with transcription factor atf e4tf3
Nucleic Acids Research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.
William S. Reznikoff - One of the best experts on this subject based on the ideXlab platform.
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Escherichia coli DNA Topoisomerase I Copurifies with Tn5 Transposase, and Tn5 Transposase Inhibits Topoisomerase I
Journal of bacteriology, 1999Co-Authors: Hesna Yigit, William S. ReznikoffAbstract:Tn5 transposase (Tnp) overproduction is lethal to Escherichia coli. Genetic evidence suggested that this killing involves titration of E. coli topoisomerase I (Topo I). Here, we present biochemical evidence that supports this model. Tn5 Tnp copurifies with Topo I while nonkilling derivatives of Tnp, Δ37Tnp and Δ55Tnp (Inhibitor [Inh]), show reduced affinity or no affinity, respectively, for Topo I. In agreement with these results, the presence of Tnp, but not Δ37 or Inh derivatives of Tnp, inhibits the DNA relaxation activity of Topo I in vivo as well as in vitro. Other proteins, including RNA polymerase, are also found to copurify with Tnp. For RNA polymerase, reduced Copurification with Tnp is observed in extracts from a topA mutant strain, suggesting that RNA polymerase interacts with Topo I and not Tnp.
Makoto Takayama - One of the best experts on this subject based on the ideXlab platform.
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Copurification of Casein Kinase II with Transcription Factor ATF/E4TF3
Nucleic acids research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.
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Copurification of casein kinase ii with transcription factor atf e4tf3
Nucleic Acids Research, 1996Co-Authors: Tadashi Wada, Toshiyuki Takagi, Yuki Yamaguchi, Hiroyuki Kawase, Masaki Hiramoto, Anwarul Ferdous, Makoto Takayama, Kevin A.w. Lee, Helen C. Hurst, Hiroshi HandaAbstract:We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. We found that the kinase interacted with ATF1 in vitro efficiently. The kinase did not bind directly to DNA. The kinase mainly phosphorylated ATF1 on serine 36, which was one of target amino acids for casein kinase (CK) II. Biological features of the kinase were the same as those of CKII and an anti-CKII serum reacted with the kinase, indicating that the kinase was CKII. Moreover, it was clearly shown that one of CKII subunits, the CKII alpha protein bound to glutathione-S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II [Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together, these results suggest that ATF/E4TF3 may recruit the CKII activity to a transcription initiation machinery and stimulate transcription.