ArticleAnalytical and bioanalytical chemistry2016
Study of the degradation of a multidrug transporter using a non-radioactive pulse chase method.
Article in Analytical and bioanalytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Unraveling the small proteome of the plant symbiontmicroLife · 2023Article
- Adaptive lifestyle of bacteria determines phage-bacteria interaction.Frontiers in microbiology · 2022Article
- Dynamic Boolean modelling reveals the influence of energy supply on bacterial efflux pump expression.Journal of the Royal Society, Interface · 2022Article
- Time dependent asymptotic analysis of the gene regulatory network of the AcrAB-TolC efflux pump system in gram-negative bacteria.Journal of mathematical biology · 2021Article
- Dynamics of chromosomal target search by a membrane-integrated one-component receptor.PLoS computational biology · 2021Article
- Article
- Quantitative analysis of newly synthesized proteins.Nature protocols · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Proteins are constantly synthesized and degraded in living cells during their growth and division, often in response to metabolic and environmental conditions. The synthesis and breakdown of proteins under different conditions reveal information about their mechanism of function. The metabolic incorporation of non-natural amino acid azidohomoalanine (AHA) and subsequent labeling via click chemistry emerged as a non-radioactive strategy useful in the determination of protein kinetics and turnover. We used the method to monitor the degradation of two proteins involved in the multidrug efflux in Escherichia coli, the inner membrane transporter AcrB and its functional partner membrane fusion protein AcrA. Together they form a functional complex with an outer membrane channel TolC to actively transport various small molecule compounds out of E. coli cells. We found that both AcrA and AcrB lasted for approximately 6 days in live E. coli cells, and the stability of AcrB depended on the presence of AcrA but not on active efflux. These results lead to new insight into the multidrug resistance in Gram-negative bacteria conferred by efflux.
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