A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity

Takahiro Nakamura, Mamoru Sugita

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Many plant pentatricopeptide repeat (PPR) proteins are known to contain a highly conserved C-terminal DYW domain whose function is unknown. Recently, the DYW domain has been proposed to play a role in RNA editing in plant organelles. To address this possibility, we prepared recombinant DYW proteins and tested their cytidine deaminase activity. However, we could not detect any activity in the assays we used. Instead, we found that the recombinant DYW domains possessed endoribonuclease activity and cleaved before adenosine residues in the RNA molecule. Some DYW-containing PPR proteins may catalyze site-specific cleavage of target RNA species.

Original languageEnglish
Pages (from-to)4163-4168
Number of pages6
JournalFEBS Letters
Volume582
Issue number30
DOIs
Publication statusPublished - Dec 24 2008

Fingerprint

Endoribonucleases
RNA
RNA Cleavage
Cytidine Deaminase
RNA Editing
Proteins
Recombinant Proteins
Organelles
Adenosine
Assays
Molecules

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity. / Nakamura, Takahiro; Sugita, Mamoru.

In: FEBS Letters, Vol. 582, No. 30, 24.12.2008, p. 4163-4168.

Research output: Contribution to journalArticle

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