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Intact ribosomes drive the formation of protein quinary structure.
- Source :
-
PloS one [PLoS One] 2020 Apr 24; Vol. 15 (4), pp. e0232015. Date of Electronic Publication: 2020 Apr 24 (Print Publication: 2020). - Publication Year :
- 2020
-
Abstract
- Transient, site-specific, or so-called quinary, interactions are omnipresent in live cells and modulate protein stability and activity. Quinary intreactions are readily detected by in-cell NMR spectroscopy as severe broadening of the NMR signals. Intact ribosome particles were shown to be necessary for the interactions that give rise to the NMR protein signal broadening observed in cell lysates and sufficient to mimic quinary interactions present in the crowded cytosol. Recovery of target protein NMR spectra that were broadened in lysates, in vitro and in the presence of purified ribosomes was achieved by RNase A digestion only after the structure of the ribosome was destabilized by removing magnesium ions from the system. Identifying intact ribosomal particles as the major protein-binding component of quinary interactions and consequent spectral peak broadening will facilitate quantitative characterization of macromolecular crowding effects in live cells and streamline models of metabolic activity.<br />Competing Interests: NO authors have competing interests.
- Subjects :
- Escherichia coli metabolism
Escherichia coli Proteins metabolism
Magnesium metabolism
Magnetic Resonance Spectroscopy methods
Nuclear Magnetic Resonance, Biomolecular methods
Protein Binding physiology
Protein Stability
Ribonuclease, Pancreatic metabolism
Protein Conformation
Proteins metabolism
Ribosomes metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 15
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 32330166
- Full Text :
- https://doi.org/10.1371/journal.pone.0232015