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
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
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.
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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 -