Molecular Cloning of a Rat 49-kDa TBP-Interacting Protein (TIP49) That Is Highly Homologous to the Bacterial RuvB

Kanemaki, Masato; Makino, Yasutaka; Yoshida, Tatsushi; Kishimoto, Toshihiko; Koga, Atsuro; Yamamoto, Kazuo; Yamamoto, Mika; Moncollin, Vincent; Egly, Jean‐Marc; Muramatsu, Masami; Tamura, Tomohiro

doi:10.1006/bbrc.1997.6729

Cited by 99 publications

(101 citation statements)

References 25 publications

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“…Independently from the experiments described above, Pontin and Reptin were also identified by virtue of their physical interaction with the transcription-associated protein β-Catenin (44,45), and with the transcription factors TBP (32,(45)(46)(47), Myc (48), E2F1 (only Pontin; 49) and ATF2 (only Reptin; 50). Subsequently, Pontin and/or Reptin were shown to bind to the promoters of transcriptional targets of c-Myc (51, 52), E2F1 (52) and NFκB (53), often along with components of the Tip60 complex.…”

Section: Transcriptional Repression By Reptin (And Pontin)mentioning

confidence: 94%

Control of transcription by Pontin and Reptin

Gallant¹

2007

Trends in Cell Biology

126

134

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Pontin and Reptin are two closely related members of the AAA+ family of DNA helicases. They have roles in diverse cellular processes, including the response to DNA double-strand breaks and the control of gene expression. The two proteins share residence in different multiprotein complexes, such as the Tip60, Ino80, SRCAP and Uri1 complexes in animals, which are involved (directly or indirectly) in transcriptional regulation, but they also function independently from each other. Both Reptin and Pontin repress certain transcriptional targets of Myc, but only Reptin is required for the repression of specific ?-catenin and nuclear factor-?B targets. Here, I review recent studies that have addressed the mechanisms of transcriptional control by Pontin and Reptin. 1Trends in Cell Biology 2007, 17(4): 187-192. Control of transcription by Pontin and ReptinPeter Gallant Zoologisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland; email: gallant@zool.unizh.ch; phone: +41446354812. AbstractPontin and Reptin are two closely related members of the AAA+ family of DNA helicases. They play roles in diverse cellular processes, including the response to DNA double-strand breaks and the control of gene expression. The two proteins share residence in different multi-protein complexes, such as the Tip60-, Ino80-, SRCAP-and Uri1-complexes in animals which are (directly or indirectly) involved in transcriptional regulation, but they also function independently from each other. Both Reptin and Pontin repress certain transcriptional targets of Myc, but only Reptin is required for the repression of specific β-Catenin and nuclear factor-κB targets. Here, I review recent studies that have addressed the mechanisms of transcriptional control by Pontin and Reptin.

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Section: Transcriptional Repression By Reptin (And Pontin)mentioning

confidence: 94%

Control of transcription by Pontin and Reptin

Gallant¹

2007

Trends in Cell Biology

126

134

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“…In addition, Pontin/ Reptin participate in complexes important for SnoRNA biogenesis (R2TP complex) and telomere maintenance (Telomerase core complex). 3 Finally, Pontin interacts directly with the TATA-binding protein, 4 and acts as co-factor for specific transcription factors and oncoproteins, such as c-Myc 5 and β-catenin, 6 both of which play essential roles in regulating hematopoietic and other stem cells. These multiple interactions of Pontin/Reptin suggest an essential physiological role, and studies in S. Cerevisiae have demonstrated that yeast orthologs of both Reptin and Pontin are required for cell viability without overall shutdown of transcription.…”

Section: Introductionmentioning

confidence: 99%

Pontin is essential for murine hematopoietic stem cell survival

et al. 2012

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© F e r r a t a S t o r t i F o u n d a t i o n © F e r r a t a S t o r t i F o u n d a t i o nMethods). Western blotting was performed on cell/tissue extracts (Online Supplementary Appendix) using Tip48, Tip49 19, PCNA (Sigma) and β-tubulin (Sigma) antibodies as described. 20 Results and DiscussionTo address the physiological role of Pontin we first generated a Ruvbl1 null allele by targeting the mouse germline (Online Supplementary Figure S1). Intercrossing of Ruvbl1 +/-mice did not generate any viable offspring, and no postimplantation Ruvbl1 -/-embryos could be retrieved ( Figure 1A). A few Ruvbl1 -/-blastocysts were identified. However, upon culturing, which results in outgrowth of the pluripotent inner cell mass, no proliferating cultures were observed to be Ruvbl1 -/-. We conclude from this that Pontin is required for embryogenesis at a very early stage, possibly involving the proliferation of pluripotent inner mass cells.To address the role of Pontin after development, we analyzed the Pontin and Reptin expression patterns in the adult mouse and selected cell lines. Overall, the expression of Pontin, but not of Reptin, correlated with that of proliferating cell nuclear antigen (PCNA), consistent with Pontin playing a specific role in cell proliferation. In particular, we found Pontin to be highly expressed in hematopoietic tissues (bone marrow, spleen, thymus, lymph nodes), as well as pluripotent cells/tissues (ES cells, testis), with low levels in liver, brain and lung ( Figure 1B). To address Pontin function in the hematopoietic system, a conditional Ruvbl1 allele (Online Supplementary Figure S1) © F e r r a t a S t o r t i F o u n d a t i o n © F e r r a t a S t o r t i F o u n d a t i o ndays post-injection, surviving Pontin cKO mice displayed a massive loss of bone marrow cellularity ( Figure 1E). This involved the coordinated loss of myeloid and lymphoid cells ( Figure 1E) and was preceeded by the complete loss of Lin -Sca-1 + c-Kit + (LSK) HSCs ( Figure 1F). To determine whether the observed effects could be attributed to an intrinsic hematopoietic requirement for Pontin, we transplanted CD45.2 Pontin cKO and Pontin Con bone marrow noncompetitively into irradiated CD45.1/2 recipients. Subsequent polyIC induction resulted in loss of hematopoietic cells ( Figure 1G and H) and lethality ( Figure 1I) Figure 2B-E), and a very high proportion of the remaining Pontin cKO HSCs were apoptotic, as measured by staining for AnnexinV and intracellular DNA ( Figure 2F). From this we conclude that Pontin is required for HSC viability and that in its absence HSCs undergo apoptosis.These results demonstrate an essential role for Pontin in early mammalian development, consistent with its presence in multiple complexes carrying out essential cellular functions. In addition, the definitive hematopoietic system in general, and HSCs in particular, were critically dependent on Pontin for its maintenance, with HSC apoptosis and depletion being an immediate consequence of Ruvbl1 inactivation. This is in contras...

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“…These two factors form a large motor protein complex to promote branch migration at Holliday junctions at the late stages of homologous recombination. The p50/p47 and RuvB proteins share highly conserved Walker domains (A and B), indicative of proteins that bind nucleotide triphosphates (10,13). Based on this, p50 and p47 were proposed to be the eukaryotic homologues of the RuvB DNA helicase.…”

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confidence: 99%

“…First, a 49-kDa protein isolated from rat liver nuclear extracts was found to interact with TATA-binding protein (TBP) (13). The 49-kDa protein, referred to as TIP49a (TBP-interacting protein) was identical to p50 and was enriched in the testes.…”

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confidence: 99%

The Saccharomyces cerevisiae RuvB-like Protein, Tih2p, Is Required for Cell Cycle Progression and RNA Polymerase II-directed Transcription

Lim¹,

Kimata²,

Ohdate³

et al. 2000

Journal of Biological Chemistry

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Two highly conserved RuvB-like putative DNA helicases, p47/TIP49b and p50/TIP49a, have been identified in the eukaryotes. Here, we study the function of Saccharomyces cerevisiae TIH2, which corresponds to mammalian p47/TIP49b. Tih2p is required for vegetative cell growth and localizes in the nucleus. Immunoprecipitation analysis revealed that Tih2p tightly interacts with Tih1p, the counterpart of mammalian p50/TIP49a, which has been shown to interact with the TATA-binding protein and the RNA polymerase II holoenzyme complex. Furthermore, the mutational study of the Walker A motif, which is required for nucleotide binding and hydrolysis, showed that this motif plays indispensable roles in the function of Tih2p. When a temperature-sensitive tih2 mutant, tih2-160, was incubated at the nonpermissive temperature, cells were rapidly arrested in the G 1 phase. Northern blot analysis revealed that Tih2p is required for transcription of G 1 cyclin and of several ribosomal protein genes. The similarities between the mutant phenotypes of tih2-160 and those of taf145 mutants suggest a role for TIH2 in the regulation of RNA polymerase II-directed transcription.One of the common post-translational modifications of nuclear and cytosolic proteins in eukaryotes is the addition of N-acetylglucosamine residues O-linked (O-GlcNAc) 1 to serine and threonine residues. A number of physiologically or structurally important proteins have thus far been shown to contain O-GlcNAc, including the largest subunit of RNA polymerase II (RNAP II) (1), transcription factors such as Sp1 and hepatocyte nuclear factor 1 (2-4), nuclear pore proteins (5, 6) and chromatin-associated proteins (7). To study nuclear factors involved in nuclear transport and other nuclear events, we previously performed an in vitro binding assay of a rat liver nuclear matrix fraction using a wheat germ agglutinin affinity column (8).Several O-GlcNAc-containing proteins such as nucleoporins as well as nonglycosylated proteins like importin ␤ were isolated (9). Two RuvB-like proteins, p50 (9) and p47 (10), were also isolated by this method probably because of their interaction with O-GlcNAc-bearing proteins. RuvB is a prokaryotic DNA helicase, and its helicase activity and DNA binding affinity are enhanced by interaction with RuvA (11,12). These two factors form a large motor protein complex to promote branch migration at Holliday junctions at the late stages of homologous recombination. The p50/p47 and RuvB proteins share highly conserved Walker domains (A and B), indicative of proteins that bind nucleotide triphosphates (10, 13). Based on this, p50 and p47 were proposed to be the eukaryotic homologues of the RuvB DNA helicase. Indeed, p50 and p47 are present in a wide range of eukaryotes ranging from yeast to mammals, suggesting that this basic helicase activity may be conserved among the eukaryotes.In addition to recombination, transient unwinding of the DNA duplex is required in many cellular processes such as replication, transcription, and DNA repair. To accommodate ...

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Molecular Cloning of a Rat 49-kDa TBP-Interacting Protein (TIP49) That Is Highly Homologous to the Bacterial RuvB

Cited by 99 publications

References 25 publications

Control of transcription by Pontin and Reptin

Control of transcription by Pontin and Reptin

Pontin is essential for murine hematopoietic stem cell survival

The Saccharomyces cerevisiae RuvB-like Protein, Tih2p, Is Required for Cell Cycle Progression and RNA Polymerase II-directed Transcription

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