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 language | English |
|---|---|
| Pages (from-to) | 4163-4168 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 582 |
| Issue number | 30 |
| DOIs | |
| Publication status | Published - Dec 24 2008 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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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 journal › Article
}
TY - JOUR
T1 - A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity
AU - Nakamura, Takahiro
AU - Sugita, Mamoru
PY - 2008/12/24
Y1 - 2008/12/24
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=57149118430&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2008.11.017
DO - 10.1016/j.febslet.2008.11.017
M3 - Article
VL - 582
SP - 4163
EP - 4168
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 30
ER -