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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Exteins

 
 
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High impact information on Exteins

  • CPS was still triggered by rapamycin when FKBP and FRB occupied one or both of the extein positions [1].
  • These results demonstrate that interaction of calmodulin and M13 triggers the refolding of intein, which induces the protein splicing, thereby folding the ligated extein correctly for yielding the EGFP fluorophore [2].
  • Such a screening system detects even low levels of protein splicing and we have used it to show that protein splicing of the RecA intein is compatible with any amino acid in the extein position adjacent to the N-terminal splice junction [3].
  • One precursor structure revealed that the N-terminal junction of the introduced extein polypeptide forms an intermediate containing a five-membered thiazolidine ring [4].

References

  1. Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. Mootz, H.D., Blum, E.S., Tyszkiewicz, A.B., Muir, T.W. J. Am. Chem. Soc. (2003) [Pubmed]
  2. A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing. Ozawa, T., Nogami, S., Sato, M., Ohya, Y., Umezawa, Y. Anal. Chem. (2000) [Pubmed]
  3. An in vivo screening system against protein splicing useful for the isolation of non-splicing mutants or inhibitors of the RecA intein of Mycobacterium tuberculosis. Lew, B.M., Paulus, H. Gene (2002) [Pubmed]
  4. Protein splicing: its discovery and structural insight into novel chemical mechanisms. Anraku, Y., Mizutani, R., Satow, Y. IUBMB Life (2005) [Pubmed]
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