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Ate1  -  arginyltransferase 1

Mus musculus

Synonyms: AI225793, AW547406, Arginine-tRNA--protein transferase 1, Arginyl-tRNA--protein transferase 1, Arginyltransferase 1, ...
 
 
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High impact information on Ate1

  • Increased levels of glutathione S-transferase (GST; RX:glutathione R-transferase; EC 2.5.1.18) mRNA, protein, and activity in tumor biopsy samples and in drug-resistant cultured cells are associated with resistance to anticancer drugs [1].
  • The predicted amino acid sequence of the antigen specified by these cDNAs shows striking homology with class mu isozymes of mammalian glutathione S-transferases (RX:glutathione R-transferase, EC 2.5.1.18) [2].
  • Purified isoforms of arginyltransferase that contain the alternative first exons differentially arginylate these proteins in extract from ATE1(-/-) embryos, suggesting that specific isoforms may have distinct functions [3].
  • Point mutations of the residues in the predicted regions of functional importance resulted in changes in enzymatic activity, including complete inactivation of mouse Ate1; other mutations altered its substrate specificity [4].
  • Through biochemical analyses, we show that N-terminal cysteine, in contrast to N-terminal aspartate and glutamate, is oxidized before its arginylation by R-transferase, suggesting that the arginylation branch of the N-end rule pathway functions as an oxygen sensor [5].
 

Analytical, diagnostic and therapeutic context of Ate1

  • Here, we used sequence analysis to detect the evolutionary relationship between the Ate1 family and bacterial FemABX family of aminoacyl-tRNA-peptide transferases, and to predict the functionally important residues in arginyltransferases, which were then used to construct a panel of mutants for further molecular dissection of mouse Ate1 [4].

References

  1. Expression of recombinant glutathione S-transferase pi, Ya, or Yb1 confers resistance to alkylating agents. Puchalski, R.B., Fahl, W.E. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  2. Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase. Smith, D.B., Davern, K.M., Board, P.G., Tiu, W.U., Garcia, E.G., Mitchell, G.F. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  3. Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms. Hu, R.G., Brower, C.S., Wang, H., Davydov, I.V., Sheng, J., Zhou, J., Kwon, Y.T., Varshavsky, A. J. Biol. Chem. (2006) [Pubmed]
  4. Molecular dissection of arginyltransferases guided by similarity to bacterial peptidoglycan synthases. Rai, R., Mushegian, A., Makarova, K., Kashina, A. EMBO Rep. (2006) [Pubmed]
  5. An essential role of N-terminal arginylation in cardiovascular development. Kwon, Y.T., Kashina, A.S., Davydov, I.V., Hu, R.G., An, J.Y., Seo, J.W., Du, F., Varshavsky, A. Science (2002) [Pubmed]
 
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