ArticleNucleic acids research2012
A transposase strategy for creating libraries of circularly permuted proteins.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 1,055 citations in OpenAlex.
- Targeted insertional mutagenesis libraries for deep domain insertion profiling.Nucleic acids research · 2020Article
- Protein tolerance to random circular permutation correlates with thermostability and local energetics of residue-residue contacts.Protein engineering, design & selection : PEDS · 2019Article
- Article
- A Split Transcriptional Repressor That Links Protein Solubility to an Orthogonal Genetic Circuit.ACS synthetic biology · 2018Article
- Circular permutation profiling by deep sequencing libraries created using transposon mutagenesis.Nucleic acids research · 2018Article
- Development of novel metabolite-responsive transcription factors via transposon-mediated protein fusion.Protein engineering, design & selection : PEDS · 2018Article
- Tolerance of a Knotted Near-Infrared Fluorescent Protein to Random Circular Permutation.Biochemistry · 2016Article
- The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation.ACS synthetic biology · 2016Article
- Transposon for protein engineering.Mobile genetic elements · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A simple approach for creating libraries of circularly permuted proteins is described that is called PERMutation Using Transposase Engineering (PERMUTE). In PERMUTE, the transposase MuA is used to randomly insert a minitransposon that can function as a protein expression vector into a plasmid that contains the open reading frame (ORF) being permuted. A library of vectors that express different permuted variants of the ORF-encoded protein is created by: (i) using bacteria to select for target vectors that acquire an integrated minitransposon; (ii) excising the ensemble of ORFs that contain an integrated minitransposon from the selected vectors; and (iii) circularizing the ensemble of ORFs containing integrated minitransposons using intramolecular ligation. Construction of a Thermotoga neapolitana adenylate kinase (AK) library using PERMUTE revealed that this approach produces vectors that express circularly permuted proteins with distinct sequence diversity from existing methods. In addition, selection of this library for variants that complement the growth of Escherichia coli with a temperature-sensitive AK identified functional proteins with novel architectures, suggesting that PERMUTE will be useful for the directed evolution of proteins with new functions.
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