1994 Fiscal Year Final Research Report Summary
Study on the post-transcriptional regulators of cyanobacteria and chloroplasts
| Project/Area Number |
04454003
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
遺伝学
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| Research Institution | Nagoya University |
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Principal Investigator |
SUGITA Mamoru Nagoya Univ., Center Gene Research, Associate Prof., 遺伝子実験施設, 助教授 (70154474)
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| Co-Investigator(Kenkyū-buntansha) |
WAKASUGI Tatsuya Nagoya Univ., Center Gene Research, Assistant Prof., 遺伝子実験施設, 助手 (10212317)
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| Project Period (FY) |
1992 – 1994
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| Keywords | RNA-binding protein / RNA-binding domain / Cyanobacteria / Chloroplast / Post-transcripnal regulation / Gene |
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| Research Abstract |
1.The unicellular cyanobacterium, Synechococcus sp. PCC 6301 has two proteins containing an RNA-binding domain homologous to the chloroplast counterparts. This is the first evidence of RNA-binding proteins (RNPs) in prokaryotes and confirms that chloroplast RNPs are of cyanobacterial origin.
2.Analysis of the genes encoding chloroplast RNPs from tobacco and Arabidopsis thaliana indicated that chloroplast RNPs can be categorized into three groups.
3.Chloroplast RNPs were demonstrated to be associated with a variety of chloroplast mRNA species, non-ribosomal 16S rRNA and intron-containing pre-tRNAs as stable RNA-protein complexes. This observation strongly suggests that the chloroplast RNPs are involved in RNA processing and RNA stability.
4.We discovered novel types of RNA-binding proteins. These novel proteins contain an N-terminal RNA-binding domain and C-terminal glycine-rich domain, therefore they are named RGP (RNA-binding Glycine-rich Proteins). RGP proteins are possibly involved in post-transcriptional regulation in nucleus.
5.Based on the RNA-binding domain structures and nucleic acids-binding properties, we discussed evolutionary relationship of the above three types of RNA-binding proteins.
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