Development of a reporter peptide that catalytically produces a fluorescent signal through [alpha]-complementation

In [alpha]-complementation, inactive N-terminal ([alpha]-domain) and C-terminal ([omega]-domain) fragments of [beta]-galactosidase associate to reconstitute the active protein. To date, the effect of [alpha]-domain size on [alpha]-complementation activity has not been systematically investigated. In...

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Bibliographic Details
Published in:Protein science 2015-05, Vol.24 (5), p.599
Main Authors: Nishiyama, Kotaro, Ichihashi, Norikazu, Kazuta, Yasuaki, Yomo, Tetsuya
Format: Article
Language:English
Subjects:
Bacteriology
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Summary:In [alpha]-complementation, inactive N-terminal ([alpha]-domain) and C-terminal ([omega]-domain) fragments of [beta]-galactosidase associate to reconstitute the active protein. To date, the effect of [alpha]-domain size on [alpha]-complementation activity has not been systematically investigated. In this study, we compared the complementation activities of [alpha]-domains of various sizes using an in vitro system. We found that the complementation activities are similar for [alpha]-domains comprising between 45 and 229 N-terminal residues but are significantly decreased for those containing less than 37 residues. However, these smaller [alpha]-domains (15 and 25 residues) exhibited sufficient [alpha]-complementation activity for application as reporters.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.2667