| Project/Area Number |
11680798
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neuroscience in general
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| Research Institution | NATIONAL INSTITUTE OF INFECTIOUS DESEASES |
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Principal Investigator |
KASAI Masataka NATIONAL INSTITUTE OF INFECTIOUS DISEASES, IMMUNOLOGY, SENIOR RESEARCHER, 免疫部, 主任研究員 (10142134)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2000: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1999: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | RP58 PROTEIN / TRANSCRIPTIONAL REGULATION / HETEROCHROMATIN / DNA結合蛋白 / 転写抑制因子 |
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| Research Abstract |
We have isolated a novel protein sharing homology with the POZ domain, an approximately 120-amino acid domain present generally at the NH2 termini of a number of zinc finger proteins, including the human BCL-6 protein. By using a binding site selection technique (CAST), a high affinity binding site of the protein was determined to be (A/C)ACATCTG(G/T)(A/C), containing the E box core sequence motif. The protein was shown to repress transcription from a promoter linked to its target sequences and was hence named RP58 (Repressor Protein with a predicted molecular mass of 58 kDa). Immunogold electron microscopic study revealed that almost all RP58 is localized in condensed chromatin regions. These observations demonstrate for the first time that a protein mediating a sequence-specific transcriptional repression associates with highly condensed chromatin. We suggest that RP58 may be involved in a molecular link between sequence-specific transcriptional repression and the organization of chromosomes in the nucleus. RP58 is highly synthesized in brain and also localized in condensed chromatin regions, suggesting a role in transcriptional repression in the central nervous system. We also found that Dnmt3a, DNA methyltransferase repressing transcription, specifically interacts with RP58.
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