ArticleMolecular microbiology2009
Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma.
Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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
21 citing papers in PubMed, 27 citations in OpenAlex.
- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- Combinatorial metabolic engineering enables high yield production of α-arbutin from sucrose by biocatalysis.Applied microbiology and biotechnology · 2023Article
- Bacterial degrons in synthetic circuits.Open biology · 2022Review
- Improving the Robustness of Engineered Bacteria to Nutrient Stress Using Programmed Proteolysis.ACS synthetic biology · 2022Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Widespread ribosome stalling in a genome-reduced bacterium and the need for translational quality control.iScience · 2021Article
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
- Impact of C-terminal amino acid composition on protein expression in bacteria.Molecular systems biology · 2020Article
- Essential metabolism for a minimal cell.eLife · 2019Article
- HspQ Functions as a Unique Specificity-Enhancing Factor for the AAA+ Lon Protease.Molecular cell · 2017Article
- Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Nature communications · 2016Article
- Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Nature reviews. Microbiology · 2016Review
- Degradation of SsrA-tagged proteins in streptococci.Microbiology (Reading, England) · 2015Article
- Review
- Tunable protein degradation in bacteria.Nature biotechnology · 2014Article
- Distinct tmRNA sequence elements facilitate RNase R engagement on rescued ribosomes for selective nonstop mRNA decay.Nucleic acids research · 2014Article
- tmRNA-mediated trans-translation as the major ribosome rescue system in a bacterial cell.Frontiers in genetics · 2014Review
- Active and accurate trans-translation requires distinct determinants in the C-terminal tail of SmpB protein and the mRNA-like domain of transfer messenger RNA (tmRNA).The Journal of biological chemistry · 2013Article
- Francisella tularensis tmRNA system mutants are vulnerable to stress, avirulent in mice, and provide effective immune protection.Molecular microbiology · 2012Article
- Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome.Methods in molecular biology (Clifton, N.J.) · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Messenger RNAs that lack in-frame stop codons promote ribosome stalling and accumulation of aberrant and potentially harmful polypeptides. The SmpB-tmRNA quality control system has evolved to solve problems associated with non-stop mRNAs, by rescuing stalled ribosomes and directing the addition of a peptide tag to the C-termini of the associated proteins, marking them for proteolysis. In Escherichia coli, the ClpXP system is the major contributor to disposal of tmRNA-tagged proteins. We have shown that the AAA+ Lon protease can also degrade tmRNA-tagged proteins, but with much lower efficiency. Here, we present a unique case of enhanced recognition and degradation of an extended Mycoplasma pneumoniae (MP) tmRNA tag by the MP-Lon protease. We demonstrate that MP-Lon can efficiently and selectively degrade MP-tmRNA-tagged proteins. Most significantly, our studies reveal that the larger (27 amino acids long) MP-tmRNA tag contains multiple discrete signalling motifs for efficient recognition and rapid degradation by Lon. We propose that higher-affinity multipartite interactions between MP-Lon and the extended MP-tmRNA tag have co-evolved from pre-existing weaker interactions, as exhibited by Lon in E. coli, to better fulfil the function of MP-Lon as the sole soluble cytoplasmic protease responsible for the degradation of tmRNA-tagged proteins.
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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.