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- Li, Shuqi, et al.
(författare)
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Rtt105 functions as a chaperone for replication protein A to preserve genome stability
- 2018
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Ingår i: EMBO Journal. - : Wiley-VCH Verlagsgesellschaft. - 0261-4189 .- 1460-2075. ; 37:17
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Tidskriftsartikel (refereegranskat)abstract
- Generation of single-stranded DNA (ssDNA) is required for the template strand formation during DNA replication. Replication Protein A (RPA) is an ssDNA-binding protein essential for protecting ssDNA at replication forks in eukaryotic cells. While significant progress has been made in characterizing the role of the RPA-ssDNA complex, how RPA is loaded at replication forks remains poorly explored. Here, we show that the Saccharomyces cerevisiae protein regulator of Ty1 transposition 105 (Rtt105) binds RPA and helps load it at replication forks. Cells lacking Rtt105 exhibit a dramatic reduction in RPA loading at replication forks, compromised DNA synthesis under replication stress, and increased genome instability. Mechanistically, we show that Rtt105 mediates the RPA-importin interaction and also promotes RPA binding to ssDNA directly in vitro, but is not present in the final RPA-ssDNA complex. Single-molecule studies reveal that Rtt105 affects the binding mode of RPA to ssDNA These results support a model in which Rtt105 functions as an RPA chaperone that escorts RPA to the nucleus and facilitates its loading onto ssDNA at replication forks.
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| 3. |
- Li, Kexue, et al.
(författare)
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Directional emissions from perovskite nanocrystals thin film enabled by metasurface integration through one step spin-coating process
- 2023
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Ingår i: Nano Research. - : Springer Science and Business Media LLC. - 1998-0124 .- 1998-0000. ; 16:5, s. 7646-7653
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Tidskriftsartikel (refereegranskat)abstract
- Advances in thin film light-emitting devices have fueled the rapid growth of a new class of solid-state lighting devices, featuring low fabrication cost, high quantum efficiency, and broadband spectrum coverage, etc. In contrast to the conventional inorganic semiconductors that rely on lattice matched high crystalline quality substrate, solution processable thin films eliminate the dependence on the substrate, which is highly desired for the ease and versatility of integrations with foreign medium. By taking this advantage, this work developed an ultracompact solution to control the directionality of thin film emitters using integrated dielectric metasurface through one step spin-coating process. As a proof of concept, directional emissions from perovskite nanocrystal thin film, including collimated light emissions and two-dimensional beam steering, are experimentally demonstrated. Notably, our approach, where light emitters were integrated on the back side of substrate after the fabrication of metasurface, judiciously avoids any potential degradation of material optical quality caused by the multi-step nanofabrication. Therefore, it can serve as a generalized scheme to engage the advantageous properties of dielectric metasurface, including the compactness, high efficiency, and beam controllability with the emerging thin film light-emitting diodes (LEDs), which is applicable to a wide range of solution processable materials, including organic light-emitting diodes, quantum-dot light emitting diodes, polymer LEDs, and perovskite LEDs, opening up new pathways to develop low-cost and ultra-compact solid state light sources with versatile beams characteristics. [Figure not available: see fulltext.].
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- Patcha Brodin, Veronika, et al.
(författare)
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Differential inside-out activation of β2 integrins by leukotriene B4 and fMLP in human neutrophils
- 2004
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Ingår i: Experimental Cell Research. - : Elsevier BV. - 0014-4827 .- 1090-2422. ; 300:2, s. 308-319
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Tidskriftsartikel (refereegranskat)abstract
- We have investigated how LTB4, an endogenous chemoattractant encountered early in the inflammatory process, and fMLP, a bacteria-derived chemotactic peptide emanating from the site of infection, mediate inside-out regulation of the β2-integrin. The role of the two chemoattractants on β2-integrin avidity was investigated by measuring their effect on β2-integrin clustering and surface mobility, whereas their effect on β2-integrin affinity was measured by the expression of a high affinity epitope, a ligand-binding domain on β2-integrins, and by integrin binding to s-ICAM. We find that the two chemoattractants modulate the β2-integrin differently. LTB4 induces an increase in integrin clustering and surface mobility, but only a modest increase in integrin affinity. fMLP evokes a large increase in β2-integrin affinity as well as in clustering and mobility. Lipoxin, which acts as a stop signal for the functions mediated by pro-inflammatory agents, was used as a tool for further examining the inside-out mechanisms. While LTB4-induced integrin clustering and mobility were inhibited by lipoxin, only a minor inhibition of fMLP-induced β2-integrin avidity and no inhibition of integrin affinity were detected. The different modes of the inside-out regulation of β2-integrins suggest that distinct mechanisms are involved in the β2-integrin modulation induced by various chemoattractants.
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