4.5 Article

Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme

Journal

FEBS LETTERS
Volume 580, Issue 7, Pages 1853-1858

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.02.045

Keywords

protein splicing; intein; segmental isotopic labelling; NMR

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Protein trans-splicing by the naturally split intein of the gene dnaE from Nostoc punctiforme (Npu DnaE) was demonstrated here with non-native exteins in Escherichia coli. Npu DnaE possesses robust trans-splicing activity with an efficiency of > 98%, which is superior to that of the DnaE intein from Synechocystis sp. strain PCC6803 (Ssp DnaE). Both the N- and C-terminal parts of the split Npu DnaE intein can be substituted with the corresponding fragment of Ssp DnaE without loss of trans-splicing activity. Protein splicing with the Npu DnaE(N) is also more tolerant of amino acid substitutions in the C-terminal extein sequence. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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