TIP49, Homologous to the Bacterial DNA Helicase RuvB, Acts as an Autoantigen in Human

Makino, Yasutaka; Mimori, Tsuneyo; Koike, Chika; Kanemaki, Masato; Kurokawa, Yumiko; Inoue, Satoshi; Kishimoto, Toshihiko; Tamura, Tomohiro

doi:10.1006/bbrc.1998.8504

Cited by 39 publications

(42 citation statements)

References 26 publications

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“…have shown that the individual human TIP48 and TIP49 proteins are very weak ATPases (16,33), but it contradicts earlier work suggesting that each protein can independently hydrolyze ATP (25,26). The rate of ATP hydrolysis for the TIP48/TIP49 complex was low when compared to many other ATPases but similar to that seen for other AAA ϩ proteins (7,8).…”

Section: Discussionmentioning

confidence: 78%

“…The U3 and U8 snoRNPs both undergo a stabilization event during biogenesis, suggesting that the snoRNP is remodelled or restructured during assembly (29,42). This rearrangement is predicted to coincide with the release of any remaining pre-snoRNP factors and the formation of the mature snoRNP (29,42).TIP48 (also known as Rvb2p, RuvBL2, TIP49b, Reptin, TAP54b, Tih2p, or p50) and TIP49 (also known as Rvb1p, RuvBL1, TIP49a, Pontin, TAP54a, Tih1p, or p55) are two related AAA ϩ proteins linked to a number of important events in eukaryotes, including transcription, histone remodelling, and snoRNP assembly (6,17,18,25,26,32,34,39,42). AAA ϩ proteins function in a wide variety of processes in the cell and generally function in the structural remodelling and unfolding of proteins and protein complexes (7,14).…”

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confidence: 99%

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Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

McKeegan

Debieux

Watkins

2009

Molecular and Cellular Biology

111

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The box C/D small nucleolar RNPs (snoRNPs) are essential for the processing and modification of rRNA. TIP48 and TIP49 are two related AAA ؉ proteins that are essential for the formation of box C/D snoRNPs. These proteins are key components of the pre-snoRNP complexes, but their exact role in box C/D snoRNP biogenesis is largely uncharacterized. Here we report that TIP48 and TIP49 interact with one another in vitro, and only the TIP48/TIP49 complex, but not the individual proteins, possesses significant ATPase activity. Loss of TIP48 and TIP49 results in a change in pre-snoRNA levels and a loss of U3 snoRNA signal in the Cajal body. We show that TIP48 and TIP49 make multiple interactions with core snoRNP proteins and biogenesis factors and that these interactions are often regulated by the presence of ATP. Furthermore, we demonstrate that TIP48 and TIP49 efficiently bridge interactions between the core box C/D proteins NOP56 or NOP58 and 15.5K. Our data imply that the snoRNP assembly factor NUFIP can regulate the interactions between TIP48 and TIP49 and the core box C/D proteins. We suggest that snoRNP assembly involves an intricate series of interactions that are mediated/regulated by bridging factors and chaperones.In the eukaryotic nucleolus, small nucleolar RNAs (snoRNAs) are involved in the processing and modification of rRNA (1,20,38). The H/ACA snoRNAs and box C/D snoRNAs function as sequence-specific guides to direct the isomerization of uridine to pseudouridine and the 2Ј-O methylation of rRNA, (1,20,38). A subset of box C/D snoRNAs that includes U3, U8, and U14 box C/D snoRNAs is essential for rRNA processing. These snoRNAs base pair with specific regions of the pre-rRNA and have been proposed to function as RNA chaperones by regulating rRNA folding (36). Box C/D snoRNAs contain a conserved box C/D motif which is involved in the binding of the four core proteins, 15.5K, NOP56, NOP58, and the methyltransferase fibrillarin (10). The core proteins assemble onto the snoRNA in a stepwise manner with 15.5K first binding to the k-turn element in the box C/D motif followed by the recruitment of the remaining core proteins into the complex (41,45).Most box C/D snoRNAs are encoded within the introns of protein-coding genes and are processed from the spliced intron lariat (9,19,21,38). In contrast, a subset of box C/D snoRNAs, including U3, U8, and U13, are independently transcribed by RNA polymerase II (9, 28, 46). The initial transcripts of these genes contain an m 7 G cap and a short 3Ј extension. During snoRNP biogenesis the m 7 G cap is converted into an m 3 G cap and the 3Ј extension is removed by exonucleases (9, 28, 46). The maturation of the snoRNA and the assembly of the snoRNP is an intricate process involving the dynamic and temporal association of numerous factors in a large multiprotein pre-snoRNP complex (29,42,43). These factors include proteins linked to snoRNP assembly (TIP48, TIP49, NUFIP, TAF9, NOP17, and BCD1), molecular chaperones (HSP90 and HSC70), nucleocytoplasmic transport factors (PHAX, ...

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Section: Discussionmentioning

confidence: 78%

mentioning

confidence: 99%

Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

McKeegan

Debieux

Watkins

2009

Molecular and Cellular Biology

111

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“…Despite a large number of reports analyzing Pontin functions, a relatively few groups have analyzed Pontin cellular distribution (Bauer et al 1998;Holzmann et al 1998;Makino et al 1998;Salzer et al 1999). However, outcomes of these studies have been inconsistent.…”

Section: Discussionmentioning

confidence: 99%

“…Pontin localization has been elusive and different groups referred to diverse localization based on the antibody and/or fixation conditions used (Bauer et al 1998;Holzmann et al 1998;Makino et al 1998;Salzer et al 1999). Moreover, a GFP-tag on either end of the protein prevents Pontin localization to the nucleus (data not shown) and thus impairs studying the intranuclear distribution.…”

Section: Intracellular Localization Of Pontinmentioning

confidence: 99%

Pontin is localized in nucleolar fibrillar centers

et al. 2008

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“…Two eukaryotic subfamilies of highly conserved RuvBlike proteins. A, amino acid sequence identities among human p47 (hp47/hTIP49b) (22), mouse p47 (mp47) (10), Tih2p, human p50 (hTIP49a/hRUVBL1) (19,57), rat p50 (rp50/rTIP49a) (9, 13), and Tih1p are shown along with the percent identities. B, TIH2 is essential for mitotic vegetative cell growth and cannot be complemented by the mammalian p47 or p50.…”

Section: Tih2mentioning

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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TIP49, Homologous to the Bacterial DNA Helicase RuvB, Acts as an Autoantigen in Human

Cited by 39 publications

References 26 publications

Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

Pontin is localized in nucleolar fibrillar centers

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

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TIP49, Homologous to the Bacterial DNA Helicase RuvB, Acts as an Autoantigen in Human

Cited by 39 publications

References 26 publications

Evidence that the AAA+Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

Evidence that the AAA+Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

Pontin is localized in nucleolar fibrillar centers

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

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Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis

Evidence that the AAA⁺Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis