Interactions with RNA/DNA of proteins involved in the regulation of transcription, translation and telomere elongation.

Takako Ohyama, Ayako Furukawa, Tatsuya Miyoshi, Yuusuke Takada, Shouta Ohgara, Kazuyuki Hiratsuka, Takao Imai, Hideyuki Okano, Hitoshi Nakagama, Takashi Nagata, Masato Katahira

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Interactions with DNA and RNA of three different proteins involved in the regulation of (1) transcription, (2) translation, and (3) telomere elongation were examined by NMR. In the first case, the combination of structural determination, dynamical analysis on the basis of relaxation data and identification of interactive surface for wild and phosphorylation-mimicking mutant proteins has given the insight on the increase of DNA-binding affinity through phosphorylation of the protein. In the second case, the arrangement of two tandem domains interacting with RNA has been determined with residual dipolar couplings and paramagnetic relaxation enhancement, which has given the idea on how the two tandem domains recognize the target RNA. In the third case, simultaneous binding of the other two tandem domains to both DNA and RNA has been analyzed with chemical shift perturbation analysis. The result has suggested that the protein composed of two tandem domains can recruit telomerase to telomere DNA.

Original languageEnglish
Pages (from-to)77-78
Number of pages2
JournalNucleic acids symposium series (2004)
Issue number51
DOIs
Publication statusPublished - 2007

ASJC Scopus subject areas

  • Medicine(all)

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