| 1. |
- Farías-Rico, José Arcadio, et al.
(författare)
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Mutational analysis of protein folding inside the ribosome exit tunnel
- 2017
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 591:1, s. 155-163
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Tidskriftsartikel (refereegranskat)abstract
- Recent work has demonstrated that cotranslational folding of proteins or protein domains in, or in the immediate vicinity of, the ribosome exit tunnel generates a pulling force on the nascent polypeptide chain that can be detected using a so-called translational arrest peptide (AP) engineered into the nascent chain as a force sensor. Here, we show that AP-based force measurements combined with systematic Ala and Trp scans of a zinc-finger domain that folds in the exit tunnel can be used to identify the residues that are critical for intraribosomal folding. Our results suggest a general approach to characterize the folded state(s) that may form as a protein domain moves progressively down the ribosome exit tunnel.
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| 2. |
- Feltre, Anna, et al.
(författare)
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The MUSE Hubble Ultra Deep Field Survey XII. Mg II emission and absorption in star-forming galaxies
- 2018
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Ingår i: Astronomy and Astrophysics. - : EDP Sciences. - 0004-6361 .- 1432-0746. ; 617
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Tidskriftsartikel (refereegranskat)abstract
- The physical origin of the near-ultraviolet Mg II emission remains an underexplored domain, unlike more typical emission lines that are detected in the spectra of star-forming galaxies. We explore the nebular and physical properties of a sample of 381 galaxies between 0.70 < z < 2.34 drawn from the MUSE Hubble Ultra Deep Survey. The spectra of these galaxies show a wide variety of profiles of the Mg II lambda lambda 2796, 2803 resonant doublet, from absorption to emission. We present a study on the main drivers for the detection of Mg II emission in galaxy spectra. By exploiting photoionization models, we verified that the emission-line ratios observed in galaxies with Mg II in emission are consistent with nebular emission from HII regions. From a simultaneous analysis of MUSE spectra and ancillary Hubble Space Telescope information through spectral energy distribution fitting, we find that galaxies with Mg II in emission have lower stellar masses, smaller sizes, bluer spectral slopes, and lower optical depth than those with absorption. This leads us to suggest that Mg II emission is a potential tracer of physical conditions that are not merely related to those of the ionized gas. We show that these differences in Mg II emission and absorption can be explained in terms of a higher dust and neutral gas content in the interstellar medium (ISM) of galaxies showing Mg II in absorption, which confirms the extreme sensitivity of Mg II to the presence of the neutral ISM. We conclude with an analogy between the Mg II doublet and the Ly alpha line that lies in their resonant nature. Further investigations with current and future facilities, including the James Webb Space Telescope, are promising because the detection of Mg II emission and its potential connection with Ly alpha could provide new insights into the ISM content in the early Universe.
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| 3. |
- Marino, Jacopo, et al.
(författare)
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Small protein domains fold inside the ribosome exit tunnel
- 2016
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 590:5, s. 655-660
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Tidskriftsartikel (refereegranskat)abstract
- Cotranslational folding of small protein domains within the ribosome exit tunnel may be an important cellular strategy to avoid protein misfolding. However, the pathway of cotranslational folding has so far been described only for a few proteins, and therefore, it is unclear whether folding in the ribosome exit tunnel is a common feature for small protein domains. Here, we have analyzed nine small protein domains and determined at which point during translation their folding generates sufficient force on the nascent chain to release translational arrest by the SecM arrest peptide, both in vitro and in live E. coli cells. We find that all nine protein domains initiate folding while still located well within the ribosome exit tunnel.
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| 4. |
- Nilsson, Ola B., et al.
(författare)
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Cotranslational Protein Folding inside the Ribosome Exit Tunnel
- 2015
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Ingår i: Cell Reports. - : Elsevier BV. - 2211-1247. ; 12:10, s. 1533-1540
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Tidskriftsartikel (refereegranskat)abstract
- At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of co-translational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
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