Abstract
We have found the gene for a translation elongation factor Tu (EF-Tu) homologue in the genome of the nematode Caenorhabditis elegans. Because the corresponding protein was detected immunologically in a nematode mitochondrial (mt) extract, it could be regarded as a nematode mt EF-Tu. The protein possesses an extension of about 57 amino acids (we call this domain 3′) at the C terminus, which is not found in any other known EF-Tu. Because most nematode mt tRNAs lack a T stem, domain 3′ may be related to this feature. The nematode EF-Tu bound to nematode T stem-lacking tRNA, but bacterial EF-Tu was unable to do so. A series of domain exchange experiments strongly suggested that domains 3 and 3′ are essential for binding to T stem-lacking tRNAs. This finding may constitute a novel example of the co-evolution of a structurally simplified RNA and the cognate RNA-binding protein, the latter having apparently acquired an additional domain to compensate for the lack of a binding site(s) on the RNA.
| Original language | English |
|---|---|
| Pages (from-to) | 21571-21577 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 276 |
| Issue number | 24 |
| DOIs | |
| Publication status | Published - 2001 Jun 15 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
An "Elongated" Translation Elongation Factor Tu for Truncated tRNAs in Nematode Mitochondria. / Ohtsuki, Takashi; Watanabe, Yoh Ichi; Takemoto, Chie; Kawai, Gota; Ueda, Takuya; Kita, Kiyoshi; Kojima, Somei; Kaziro, Yoshito; Nyborg, Jens; Watanabe, Kimitsuna.
In: Journal of Biological Chemistry, Vol. 276, No. 24, 15.06.2001, p. 21571-21577.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - An "Elongated" Translation Elongation Factor Tu for Truncated tRNAs in Nematode Mitochondria
AU - Ohtsuki, Takashi
AU - Watanabe, Yoh Ichi
AU - Takemoto, Chie
AU - Kawai, Gota
AU - Ueda, Takuya
AU - Kita, Kiyoshi
AU - Kojima, Somei
AU - Kaziro, Yoshito
AU - Nyborg, Jens
AU - Watanabe, Kimitsuna
PY - 2001/6/15
Y1 - 2001/6/15
N2 - We have found the gene for a translation elongation factor Tu (EF-Tu) homologue in the genome of the nematode Caenorhabditis elegans. Because the corresponding protein was detected immunologically in a nematode mitochondrial (mt) extract, it could be regarded as a nematode mt EF-Tu. The protein possesses an extension of about 57 amino acids (we call this domain 3′) at the C terminus, which is not found in any other known EF-Tu. Because most nematode mt tRNAs lack a T stem, domain 3′ may be related to this feature. The nematode EF-Tu bound to nematode T stem-lacking tRNA, but bacterial EF-Tu was unable to do so. A series of domain exchange experiments strongly suggested that domains 3 and 3′ are essential for binding to T stem-lacking tRNAs. This finding may constitute a novel example of the co-evolution of a structurally simplified RNA and the cognate RNA-binding protein, the latter having apparently acquired an additional domain to compensate for the lack of a binding site(s) on the RNA.
AB - We have found the gene for a translation elongation factor Tu (EF-Tu) homologue in the genome of the nematode Caenorhabditis elegans. Because the corresponding protein was detected immunologically in a nematode mitochondrial (mt) extract, it could be regarded as a nematode mt EF-Tu. The protein possesses an extension of about 57 amino acids (we call this domain 3′) at the C terminus, which is not found in any other known EF-Tu. Because most nematode mt tRNAs lack a T stem, domain 3′ may be related to this feature. The nematode EF-Tu bound to nematode T stem-lacking tRNA, but bacterial EF-Tu was unable to do so. A series of domain exchange experiments strongly suggested that domains 3 and 3′ are essential for binding to T stem-lacking tRNAs. This finding may constitute a novel example of the co-evolution of a structurally simplified RNA and the cognate RNA-binding protein, the latter having apparently acquired an additional domain to compensate for the lack of a binding site(s) on the RNA.
UR - http://www.scopus.com/inward/record.url?scp=0035877834&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035877834&partnerID=8YFLogxK
U2 - 10.1074/jbc.M011118200
DO - 10.1074/jbc.M011118200
M3 - Article
C2 - 11262399
AN - SCOPUS:0035877834
VL - 276
SP - 21571
EP - 21577
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 24
ER -