ArticleProceedings of the National Academy of Sciences of the United States of America2005
Target-directed proteolysis at the ribosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. 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, 25 citations in OpenAlex.
- A bacterial type III secretion-based protein delivery tool for broad applications in cell biology.The Journal of cell biology · 2015Article
- A tobacco etch virus protease with increased substrate tolerance at the P1' position.PloS one · 2013Article
- Localization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an Escherichia coli cell-free system.Biotechnology and bioengineering · 2011Article
- TEV protease-facilitated stoichiometric delivery of multiple genes using a single expression vector.Protein science : a publication of the Protein Society · 2010Article
- Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli.Journal of bacteriology · 2009Article
- Efficient protein depletion by genetically controlled deprotection of a dormant N-degron.Molecular systems biology · 2009Article
- Optimization of the Production of Soluble Recombinant TEV Protease in TwoAvicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Target directed proteolysis allows specific processing of proteins in vivo. This method uses tobacco etch virus (TEV) NIa protease that recognizes a seven-residue consensus sequence. Because of its specificity, proteins engineered to contain a cleavage site are proteolysed, whereas other proteins remain unaffected. Therefore, this approach can be used to study the structure and function of target proteins in their natural environment within living cells. One application is the conditional inactivation of essential proteins, which is based on the concept that a target containing a recognition site can be inactivated by coexpressed TEV protease. We have previously identified one site in the secretion factor SecA that tolerated a TEV protease site insert. Coexpression of TEV protease in the cytoplasm led to incomplete cleavage and a mild secretion defect. To improve the efficiency of proteolysis, TEV protease was attached to the ribosome. We show here that cleaving SecA under these conditions is one way of increasing the efficiency of target directed proteolysis. The implications of recruiting novel biological activities to ribosomes are discussed.
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