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Nucleic Acids Research, 2000, Vol. 28, No. 15 2866-2872
© 2000 Oxford University Press

An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing

Jee Eun Kim, Kyoung-Hee Kim, Sang Won Lee, Wongi Seol, Kiyotaka Shiba1 and Sunghoon Kim*

National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, 300 Chunchun-Dong, Changan-Ku, Suwon-Si, Kyunggi-Do 440-746, Korea and 1Department of Cell Biology, Cancer Institute, Japanese Foundation for Cancer Research, Tokyo 170-8455, Japan

The amino acid sequence of human cytoplasmic cysteinyl-tRNA synthetase (CRS) was examined by analyzing sequences of genomic and expressed sequence tag fragments. From theses analyses, a few interesting possibilities were suggested for the structure of human CRS. First, different isoforms of CRS may result from alternative splicing. Second, the largest one would comprise 831 amino acids. Third, a new exon was identified encoding an 83 amino acid domain that is homologous to parts of elongation factor-1 subunits as well as other proteins involved in protein synthesis. Northern blot analysis showed three different mRNAs for CRS (of ~3.0, 2.7 and 2.0 kb) from human testis while only the 2.7 kb mRNA was commonly detected in other tissues. Expression of the exon 2-containing transcript in testis was confirmed by RT–PCR and northern blotting. CRS containing the exon 2-encoded peptide retained catalytic activity comparable to that lacking this peptide. This peptide was responsible for the specific interaction of CRS with elongation factor-1{gamma}.

* To whom correspondence should be addressed. Tel: +82 331 290 5681; Fax: +82 331 290 5682; Email: shkim@yurim.skku.ac.kr


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