ArticleProtein science : a publication of the Protein Society2015
Development of a reporter peptide that catalytically produces a fluorescent signal through α-complementation.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Targeted DNA transposition in vitro using a dCas9-transposase fusion protein.Nucleic acids research · 2019Article
- Improved Monitoring of Low-Level Transcription inFrontiers in microbiology · 2019Article
- Translation activity of chimeric ribosomes composed ofBiochemistry and biophysics reports · 2017Article
- Combinatorial selection for replicable RNA by Qβ replicase while maintaining encoded gene function.PloS one · 2017Article
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4 authors.
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Abstract
In α-complementation, inactive N-terminal (α-domain) and C-terminal (ω-domain) fragments of β-galactosidase associate to reconstitute the active protein. To date, the effect of α-domain size on α-complementation activity has not been systematically investigated. In this study, we compared the complementation activities of α-domains of various sizes using an in vitro system. We found that the complementation activities are similar for α-domains comprising between 45 and 229 N-terminal residues but are significantly decreased for those containing less than 37 residues. However, these smaller α-domains (15 and 25 residues) exhibited sufficient α-complementation activity for application as reporters.
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