Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.

Nagata, Kyosuke; Kawase, Hiroyuki; Handa, Hiroshi; Yano, Keiichi; Yamasaki, Makari; Ishimi, Yukio; Okuda, Asuko; Kikuchi, Atsumi; Matsumoto, Ken

doi:10.1073/pnas.92.10.4279

Cited by 170 publications

(190 citation statements)

References 21 publications

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“…This region of SET contains a large acidic domain that has been described to be involved in a number of functions as for instance, DNA replication of adenovirus genome (Nagata et al, 1995) or cyclin B-cdk1 inhibition (Canela et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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We report here that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts in vitro and in vivo with the protein SET. This interaction is performed through the acidic domain of SET located at the carboxy terminal region. On analysing the functional relevance of SET-GAPDH interaction, we observed that GAPDH reverses in a dose-dependent manner, the inhibition of cyclin Bcdk1 activity produced by SET. Similarly to SET, GAPDH associates with cyclin B, suggesting that the regulation of cyclin B-cdk1 activity might be mediated not only by the interaction of GAPDH with SET but also with cyclin B. To analyse the putative role of GAPDH on cell cycle progression, HCT116 cells were transfected with a GAPDH expression vector. Results indicate that overexpression of GAPDH does not affect the timing of DNA replication but induces an increase in the number of mitosis, an advancement of the peak of cyclin B-cdk1 activity and an acceleration of cell cycle progression. All these results suggest that GAPDH might be involved in cell cycle regulation by modulating cyclin B-cdk1 activity.

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Section: Discussionmentioning

confidence: 99%

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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“…Previous studies have shown that nucleosome assembly protein-I (NAP-I) has significant amino acid sequence similarity to TAF-I, and that it can substitute for TAF-I activity in the replication of Ad core DNA (von Lindern et al 1992a;Nagata et al 1995). Nucleosome assembly protein (NAP-I), which contains three negatively charged regions, is found in various eukaryotic cells and has been shown to interact with cellular histones and to facilitate nucleosome formation (Fujii-Nakata et al 1992;Ishimi et al 1987).…”

Section: Substitution For Taf-i By Nap-imentioning

confidence: 99%

NAP‐I is a functional homologue of TAF‐I that is required for replication and transcription of the adenovirus genome in a chromatin‐like structure

et al. 1996

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Background: For the activation of replication and transcription from DNA in a chromatin structure, a variety of factors are thought to be needed that alter the chromatin structure. Template activating factor-I (TAF-I) has been identified as such a host factor required for replication of the adenovirus (Ad) genome complexed with viral basic core proteins (Ad core). TAF-I also stimulates transcription from the Ad core DNA.

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“…One protein was identified as non-muscle myosin IIA (NMIIA) and we explored further the possibility that NMIIA may be involved in virus maturation. Here we report on the identity of two of the other VP22-binding proteins as template-activating factor I a and b (TAF-Ia and -b), also named SETa and SETb (Adachi et al, 1994;Nagata et al, 1995;von Lindern et al, 1992). TAF-Ia and -b, identified originally as host factors required for adenovirus core replication, have been implicated in chromatin remodelling and were shown to promote the deposition of histones on naked DNA (Miyaji-Yamaguchi et al, 1999;.…”

Section: Introductionmentioning

confidence: 99%

Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT

Leeuwen

Okuwaki

Hong

et al. 2003

Journal of General Virology

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Affinity chromatography was used to identify cellular proteins that interact with the herpes simplex virus (HSV) tegument protein VP22. Among a small set of proteins that bind specifically to VP22, we identified TAF-I (template-activating factor I), a chromatin remodelling protein and close homologue of the histone chaperone protein NAP-1. TAF-I has been shown previously to promote more ordered transfer of histones to naked DNA through a direct interaction with histones. TAF-I, as a subunit of the INHAT (inhibitor of acetyltransferases) protein complex, also binds to histones and masks them from being substrates for the acetyltransferases p300 and PCAF. Using in vitro assays for TAF-I activity in chromatin assembly, we show that VP22 inhibits nucleosome deposition on DNA by binding to TAF-I. We also observed that VP22 binds non-specifically to DNA, an activity that is abolished by TAF-I. However, the presence of VP22 does not affect the property of INHAT in inhibiting the histone acetyltransferase activity of p300 or PCAF in vitro. We speculate that this interaction could be relevant to HSV DNA organization early in infection, for example, by interfering with nucleosomal deposition on the genome. Consistent with this possibility was the observation that overexpression of TAF-I in transfected cells interferes with the progression of HSV-1 infection.

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Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.

Cited by 170 publications

References 21 publications

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

NAP‐I is a functional homologue of TAF‐I that is required for replication and transcription of the adenovirus genome in a chromatin‐like structure

Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT

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