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Oral presentation

Correlation between RNA editing sites of plant organelle mRNAs and the three-dimensional structures of encoded proteins

Yura, Kei; Go, Michiko*

no journal, , 

DNAs of Plant Organelles undergo RNA editing, a transcript repair mechanisms. Those RNA editing sites seems to be located uniformly on pre-mature mRNA. This previous finding suggested that RNA editing has nothing to do with protein function. In this study, we challenged this idea based on our new database gathering all the known RNA editing sites combined with protein three-dimensional structures. We gathered 1923 RNA editing sites out of 365 pre-mature mRNAs. We have investigated and found a good correlation between the site undergoing RNA editing and protein three-dimensional structure. The finding may suggest mechanisms and evolution of RNA editing.

Oral presentation

PprM; A Homolog of cold shock protein in ${it Deinococcus radiodurans}$

Sato, Katsuya; Narumi, Issei; Oba, Hirofumi

no journal, , 

no abstracts in English

Oral presentation

Functional and structural analysis of secreted protein by complexation with an antibody fragment

Tamada, Taro; Arai, Shigeki; Shoyama, Yoshinari; Honjo, Eijiro; Kuroki, Ryota

no journal, , 

no abstracts in English

Oral presentation

Analysis on interactions of DNA with the novel DNA repairing protein PprA derived from Deinococcus radiodurans

Adachi, Motoyasu; Tamada, Taro; Sato, Katsuya; Yura, Kei; Narumi, Issei; Kuroki, Ryota

no journal, , 

PprA is cloned from the bacteria and the novel DNA repair protein that plays an important role in the resistance. This study is aimed to reveal the structure function relationship of PprA. The recombinant PprA protein was purified from E. coli. The interactions of PprA with DNA were analyzed by gel shift assay and gel filtration. The results showed that (1) at least 280 molecules of PprA can bound to a DNA molecule of pUC19 composed of 2686bp (2) the formation the complex of PprA and DNA depends on Mg, Ca and Sr ions at low concentration (3) the formation the complex of PprA and DNA depends on the concentration of the salt at the range of 0 to 0.4M sodium acetate. In addition, the result indicated that the complexes of PprA and DNA can form larger complex depending on the concentration of PprA molecule, when using linear double stranded DNA. This suggests that PprA may locate two terminals of a DNA molecule damaged by radiation at near distance for DNA repairing.

Oral presentation

Down-regulation of radioresitance by LexA2 in ${it Deinococcus radiodurans}$

Sato, Katsuya; Oba, Hirofumi; Sghaier, H.*; Narumi, Issei

no journal, , 

In an effort to gain an insight into the role of LexA2 of ${it Deinococcus radiodurans}$ in the radiation response mechanism, gene disruptant strains were generated and investigated. The intracellular level of RecA increased in ${it lexA1}$ and ${it lexA2}$ disruptant strains following irradiation as in the wild-type strain. These results indicated that the two LexA homologs did not possess functional overlap regarding the induction of RecA. The ${it lexA2}$ disruptant strains exhibited a much higher resistance to $$gamma$$ rays than the wild-type strain. Furthermore, a luciferase assay showed that ${it pprA}$ promoter activation was enhanced in the ${it lexA2}$ disruptant strain following $$gamma$$ irradiation. The ${it pprA}$ gene encoding the novel radiation-inducible protein PprA plays a critical role in the radioresistance of ${it D. radiodurans}$. The increase in radioresistance of the ${it lexA2}$ disruptant strain is explained in part by the enhancement of ${it pprA}$ promoter activation.

Oral presentation

Preparation and characterization of extracelluar region of Interleukin-13 receptor $$alpha$$1 chain and IL-4 receptor $$alpha$$

Honjo, Eijiro; Shoyama, Yoshinari; Tamada, Taro; Arima, Kazuhiko*; Kanaji, Sachiko*; Izuhara, Kenji*; Kuroki, Ryota

no journal, , 

The receptor binding to Interleukin (IL)-13 is composed of the IL-13 receptor $$alpha$$1 chain (IL-13R$$alpha$$1) and the IL-4 receptor $$alpha$$ chain (IL-4R$$alpha$$). In order to investigate the interaction of IL-13 with IL-13R$$alpha$$1 and IL-4R$$alpha$$, the DNA fragments coding the extracellular regions of human IL-13R$$alpha$$1 and the IL-4R$$alpha$$, containing a cytokine receptor homologous region, were fused with human Fc and expressed by silkworm-baculovirus system. Size exclusion chromatography did not reveal association between IL-13 and IL-13R$$alpha$$1 under these conditions, but the clear association of IL-13 and IL-13R$$alpha$$1 was observed after adding IL-4R$$alpha$$. This indicates that both extracellular regions of IL-13R$$alpha$$1 and IL-4R$$alpha$$ have functions, and the association between IL-13 and IL-4R$$alpha$$ increases the IL-13 affinity to IL-13R$$alpha$$1.

Oral presentation

Analysis of mutation frequency in Arabidopsis REV3 and REV1 deficient mutants

Nakagawa, Mayu; Sakamoto, Ayako; Takahashi, Shinya*; Tanaka, Atsushi; Narumi, Issei

no journal, , 

no abstracts in English

Oral presentation

Analysis of DNA polymerase $$zeta$$ and REV1 protein in Arabidopsis

Sakamoto, Ayako; Takahashi, Shinya*; Iwai, Shigenori*; Shimizu, Kikuo*

no journal, , 

no abstracts in English

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