Abstract
AlaX is the homologue of the class II alanyl-tRNA synthetase editing domain and has been shown to exhibit autonomous editing activity against mischarged tRNAAla. Here, we present the structures of AlaX from the archaeon Pyrococcus horikoshii in apo form, complexed with zinc, and with noncognate amino acid L-serine and zinc. Together with mutational analysis, we demonstrated that the conserved Thr-30 hydroxyl group located near the β-methylene of the bound serine is responsible for the discrimination of noncognate serine from cognate alanine, based on their chemical natures. Furthermore, we confirmed that the conserved Gin-584 in alanyl-tRNA synthetase, which corresponds to Thr-30 of AlaX, is also critical for discrimination. These observations strongly suggested conservation of the chemical discrimination among trans- and cis-editing of tRNAAla.
| Original language | English |
|---|---|
| Pages (from-to) | 11669-11674 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 102 |
| Issue number | 33 |
| DOIs | |
| Publication status | Published - Aug 16 2005 |
| Externally published | Yes |
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Cite this
Molecular basis of alanine discrimination in editing site. / Sokabe, Masaaki; Okada, Ayuko; Yao, Min; Nakashima, Takashi; Tanaka, Isao.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, No. 33, 16.08.2005, p. 11669-11674.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular basis of alanine discrimination in editing site
AU - Sokabe, Masaaki
AU - Okada, Ayuko
AU - Yao, Min
AU - Nakashima, Takashi
AU - Tanaka, Isao
PY - 2005/8/16
Y1 - 2005/8/16
N2 - AlaX is the homologue of the class II alanyl-tRNA synthetase editing domain and has been shown to exhibit autonomous editing activity against mischarged tRNAAla. Here, we present the structures of AlaX from the archaeon Pyrococcus horikoshii in apo form, complexed with zinc, and with noncognate amino acid L-serine and zinc. Together with mutational analysis, we demonstrated that the conserved Thr-30 hydroxyl group located near the β-methylene of the bound serine is responsible for the discrimination of noncognate serine from cognate alanine, based on their chemical natures. Furthermore, we confirmed that the conserved Gin-584 in alanyl-tRNA synthetase, which corresponds to Thr-30 of AlaX, is also critical for discrimination. These observations strongly suggested conservation of the chemical discrimination among trans- and cis-editing of tRNAAla.
AB - AlaX is the homologue of the class II alanyl-tRNA synthetase editing domain and has been shown to exhibit autonomous editing activity against mischarged tRNAAla. Here, we present the structures of AlaX from the archaeon Pyrococcus horikoshii in apo form, complexed with zinc, and with noncognate amino acid L-serine and zinc. Together with mutational analysis, we demonstrated that the conserved Thr-30 hydroxyl group located near the β-methylene of the bound serine is responsible for the discrimination of noncognate serine from cognate alanine, based on their chemical natures. Furthermore, we confirmed that the conserved Gin-584 in alanyl-tRNA synthetase, which corresponds to Thr-30 of AlaX, is also critical for discrimination. These observations strongly suggested conservation of the chemical discrimination among trans- and cis-editing of tRNAAla.
UR - http://www.scopus.com/inward/record.url?scp=23844487072&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=23844487072&partnerID=8YFLogxK
U2 - 10.1073/pnas.0502119102
DO - 10.1073/pnas.0502119102
M3 - Article
C2 - 16087889
AN - SCOPUS:23844487072
VL - 102
SP - 11669
EP - 11674
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 33
ER -