ArticleThe Journal of biological chemistry2011
Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 34 citations in OpenAlex.
- Article
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- Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Atlas: automatic modeling of regulation of bacterial gene expression and metabolism using rule-based languages.Bioinformatics (Oxford, England) · 2021Article
- Mature Luffa Leaves (Frontiers in plant science · 2017Article
- In vitro evolution of α-hemolysin using a liposome display.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.PloS one · 2013Article
- Directed Evolution of Proteins through In Vitro Protein Synthesis in Liposomes.Journal of nucleic acids · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Both β-galactosidase (GAL) and β-glucuronidase (GUS) are tetrameric enzymes used widely as reporter proteins. However, little is known about the folding and assembly of these enzymes. Although the refolding kinetics of GAL from a denatured enzyme have been reported, it is not known how the kinetics differ when coupled with a protein translation reaction. Elucidating the assembly kinetics of GAL and GUS when coupled with protein translation will illustrate the differences between these two reporter proteins and also the assembly process under conditions more relevant to those in vivo. In this study, we used an in vitro translation/transcription system to synthesize GAL and GUS, measured the time development of the activity and oligomerization state of these enzymes, and determined the rate constants of the monomer to tetramer assembly process. We found that at similar concentrations, GAL assembles into tetramers faster than GUS. The rate constant of monomer to dimer assembly of GAL was 50-fold faster when coupled with protein translation than that of refolding from the denatured state. Furthermore, GAL synthesis was found to lack the rate-limiting step in the assembly process, whereas GUS has two rate-limiting steps: monomer to dimer assembly and dimer to tetramer assembly. The consequence of these differences when used as reporter proteins is discussed.
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