ArticleNucleic acids research2000
An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Functional and pathologic association of aminoacyl-tRNA synthetases with cancer.Experimental & molecular medicine · 2022Review
- Aminoacyl-tRNA synthetases as therapeutic targets.Nature reviews. Drug discovery · 2019Review
- Unique roles of tryptophanyl-tRNA synthetase in immune control and its therapeutic implications.Experimental & molecular medicine · 2019Review
- A Flexible System for Cultivation ofArchaea (Vancouver, B.C.) · 2017Article
- Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.The Journal of biological chemistry · 2015Article
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Functional expansion of human tRNA synthetases achieved by structural inventions.FEBS letters · 2010Review
- Low conservation and species-specific evolution of alternative splicing in humans and mice: comparative genomics analysis using well-annotated full-length cDNAs.Nucleic acids research · 2008Article
- Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes.Nucleic acids research · 2006Article
- Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1.Journal of virology · 2001Article
- The renaissance of aminoacyl-tRNA synthesis.EMBO reports · 2001Review
- tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 approximately 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-1gamma.
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