ArticleJournal of the American Chemical Society2008
High-throughput selection for cellulase catalysts using chemical complementation.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 48 citations in OpenAlex.
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Synthetic biology: at the crossroads of genetic engineering and human therapeutics-a Keystone Symposia report.Annals of the New York Academy of Sciences · 2021Review
- Measurement of filter paper activities of cellulase with microplate-based assay.Saudi journal of biological sciences · 2016Article
- Methods for the directed evolution of proteins.Nature reviews. Genetics · 2015Review
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Transcriptional regulation improves the throughput of three-hybrid counter selections in Saccharomyces cerevisiae.Biotechnology journal · 2013Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways.Metabolic engineering · 2012Review
- Reiterative Recombination for the in vivo assembly of libraries of multigene pathways.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Engineering of Clostridium phytofermentans Endoglucanase Cel5A for improved thermostability.Applied and environmental microbiology · 2010Article
- Cellulase production from Pseudoalteromonas sp. NO3 isolated from the sea squirt Halocynthia rorentzi.Journal of industrial microbiology & biotechnology · 2009Article
- Protein engineering in designing tailored enzymes and microorganisms for biofuels production.Current opinion in biotechnology · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Efficient enzymatic hydrolysis of lignocellulosic material remains one of the major bottlenecks to cost-effective conversion of biomass to ethanol. Improvement of glycosylhydrolases, however, is limited by existing medium-throughput screening technologies. Here, we report the first high-throughput selection for cellulase catalysts. This selection was developed by adapting chemical complementation to provide a growth assay for bond cleavage reactions. First, a URA3 counter selection was adapted to link chemical dimerizer activated gene transcription to cell death. Next, the URA3 counter selection was shown to detect cellulase activity based on cleavage of a tetrasaccharide chemical dimerizer substrate and decrease in expression of the toxic URA3 reporter. Finally, the utility of the cellulase selection was assessed by isolating cellulases with improved activity from a cellulase library created by family DNA shuffling. This application provides further evidence that chemical complementation can be readily adapted to detect different enzymatic activities for important chemical transformations for which no natural selection exists. Because of the large number of enzyme variants that selections can now test as compared to existing medium-throughput screens for cellulases, this assay has the potential to impact the discovery of improved cellulases and other glycosylhydrolases for biomass conversion from libraries of cellulases created by mutagenesis or obtained from natural biodiversity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.