• 제목/요약/키워드: PCAF

검색결과 3건 처리시간 0.016초

Effects of Proto-oncogene Protein DEK on PCAF Localization

  • Lee, In-Seon;Lee, Seok-Cheol;Lee, Jae-Hwi;Seo, Sang-Beom
    • Biomolecules & Therapeutics
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    • 제15권2호
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    • pp.78-82
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    • 2007
  • The proto-oncogene protein DEK is a nuclear binding phosphoprotein that has been associated with various human diseases including leukemia. Histone acetylation is an important post-translational modification which plays important role in transcriptional regulation. Auto-acetylation of histone acetyltransferase PCAF results in increment of its HAT activity and facilitation of its nuclear localization. In this study, we report that DEK inhibits PCAF auto-acetylation through direct interaction. The C-terminal acidic domains of DEK are responsible for the interaction with PCAF. Using confocal microscopy, we have shown that nuclear localization of PCAF is severely inhibited by DEK. Taken together, our results suggest that DEK may be involved in various cellular signal transduction pathways accommodated by PCAF through the regulation of PCAF auto-acetylation.

해녀콩(Canavalia lineata)의 잎, 뿌리 및 도관액에서 Canavanine의 함량분석 (The Analysis of Canavanine Content in Leaves, Roots, and Xylem Exudate of Canavalia lineata)

  • 박경순
    • Journal of Plant Biology
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    • 제33권2호
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    • pp.119-126
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    • 1990
  • The content of canavanine was measured and analyzed in leaves, roots and xylem exudate of Canavalia lneata. In non-nodulated plants, the cotyledons were removed after a week of sowing and the plants were grown for 3 weeks. The quantity of canavanine measured by canavanine specific-PCAF colorimetric assay was 9-10 $\mu$mol/g fresh wt. in leaves, 5-6 $\mu$mol/g fresh wt. in roots, and 0.3-0.5 $\mu$mol/ml in xylem exudate. When free amino acids of leaves, roots, and xylem exudate were analysed by HPLC, the relative proportion of asparagine plus glycine was the highest and canavanine was high secondarily. And the relative proportion of canavanine among total free amino acids was 30-35% in leaves and roots, and 12-13% in xylem exudate. In non-nodulated plants grown for 8 weeks, the canavanine content of each part was similar to that of 3-week-old plants. By the formation of nodules, the canavanine content of leaves, roots, xylem exudate, and nodules decreased apparently. In xylem exduate, the nitrogenous compounds were also analyzed. The relative contents of NO3-, free amino acids, and ureides(allantoin and allantoic acid) were 60-80%, 20-30%, and 5%, respectively. From these results, it can be assumed that canavanine is synthesized in the root of plant and nodulation affects the canavanine content. It is obvious that canavanine is considered one of the reduced-N forms transported via xylem.

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Direct Interaction Between Akt1 and Gcn5 and its Plausible Function on Hox Gene Expression in Mouse Embryonic Fibroblast Cells

  • Oh, Ji Hoon;Lee, Youra;Kong, Kyoung-Ah;Kim, Myoung Hee
    • 대한의생명과학회지
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    • 제19권3호
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    • pp.266-269
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    • 2013
  • Hox genes encode transcription factors important for anterior-posterior body patterning at early stages of embryonic development. However, the precise mechanisms by which signal pathways are stimulated to regulate Hox gene expression are not clear. In the previous study, protein kinase B alpha (Akt1) has been identified as a putative upstream regulator of Hox genes, and Akt1 has shown to regulate Gcn5, a prototypical histone acetyltransferase (HAT), in a negative way in mouse embryonic fibroblast (MEF) cells. Since the activity of HAT such as the CBP/p300, and PCAF (a Gcn5 homolog), was down-regulated by Akt through a phosphorylation at the Akt consensus substrate motif (RXRXXS/T), the amino acid sequence of Gcn5 protein was analyzed. Mouse Gcn5 contains an Akt consensus substrate motif as RQRSQS sequence while human Gcn5 does not have it. In order to see whether Akt1 directly binds to Gcn5, immunoprecipitation with anti-Akt1 antibody was carried out in wild-type (WT) mouse embryonic fibroblast (MEF) cells, and then western blot analysis was performed with anti-Akt1 and anti-Gcn5 antibodies. Gcn5 protein was detected in the Akt1 immunoprecipitated samples of MEFs. This result demonstrates that Akt1 directly binds to Gcn5, which might have contributed the down regulation of the 5' Hoxc gene expressions in wild type MEF cells.