Substrate specificities of inteins investigated by QuickDrop-cassette mutagenesis.
intein
mutagenesis
protein ligation
protein splicing
substrate specificity
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
12
07
2020
revised:
05
08
2020
accepted:
10
08
2020
pubmed:
18
8
2020
medline:
13
5
2021
entrez:
18
8
2020
Statut:
ppublish
Résumé
Inteins catalyze self-excision from host precursor proteins while concomitantly ligating the flanking substrates (exteins) with a peptide bond. Noncatalytic extein residues near the splice junctions, such as the residues at the -1 and +2 positions, often strongly influence the protein-splicing efficiency. The substrate specificities of inteins have not been studied for many inteins. We developed a convenient mutagenesis platform termed "QuickDrop"-cassette mutagenesis for investigating the influences of 20 amino acid types at the -1 and +2 positions of different inteins. We elucidated 17 different profiles of the 20 amino acid dependencies across different inteins. The substrate specificities will accelerate our understanding of the structure-function relationship at the splicing junctions for broader applications of inteins in biotechnology and molecular biosciences.
Identifiants
pubmed: 32805768
doi: 10.1002/1873-3468.13909
doi:
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3338-3355Informations de copyright
© 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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