Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation

Protein splicing involves the excision of an internal domain from a precursor protein and the ligation of the external domains so as to generate two new proteins. Study of this process has recently been facilitated by the isolation of a precursor and a branched intermediate from a thermophilic prote...

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Bibliographic Details
Published in:The EMBO journal 1994-12, Vol.13 (23), p.5517-5522
Main Authors: Xu, M.Q., Comb, D.G., Paulus, H., Noren, C.J., Shao, Y., Perler, F.B.
Format: Article
Language:English
Subjects:
Alkalies
Amino Acid Sequence
Base Sequence
Conserved Sequence
DNA Primers
Molecular Sequence Data
Protein Processing, Post-Translational
Proteins - chemistry
Proteins - metabolism
Sequence Homology, Amino Acid
Succinimides - metabolism
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Summary:Protein splicing involves the excision of an internal domain from a precursor protein and the ligation of the external domains so as to generate two new proteins. Study of this process has recently been facilitated by the isolation of a precursor and a branched intermediate from a thermophilic protein splicing element expressed in a foreign protein context. Two aspects of protein splicing are examined in this paper. We demonstrate a succinimide at the C‐terminus of the spliced internal protein, implicating cyclization of asparagine in resolution of the branched intermediate, and we identify an alkali‐labile bond in the branched intermediate. A revised protein splicing model based on these experimental results is presented.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1994.tb06888.x