October (2018). We welcome Alex and Rosie from C. Toseland group for a research visit in the context of a iLINK project from CSIC.
September (2018). Publication uploaded to BioRxiv server. “Human CtIP forms a tetrameric dumbbell-shaped particle which binds and bridges complex DNA end structures for double-strand break repair” by Oliver J Wilkinson et al.
September (2018). 3rd Emerging Scientist Workshop SEBBM takes place in Santander, organized by Fernando Moreno.
September (2018). Fernando Moreno, Carolina Carrasco and Clara Aicart visit the Toseland group at Canterbury Univ.
September (2018). A. Martín-González leaves for a 3 month research visit at Professor T. Ando group (Nano-Life Science Institue at Kanazawa, Japan).
July (2018). F. Moreno-Herrero and C.Lopez-Pasatrana visit Lumicks Headquarters in Amsterdam.
July (2018). We welcome M. Alvarez and B. Lago for a one-month stay in our lab.
June (2018). A. Martin-Gonzalez wins the SPM Image Contest at Fuerzas y Tunel Conference, Jaca.
June (2018). A. Martin-Gonzalez talk and A. Marin-Gonzalez poster at Fuerzas y Tunel Conference, Jaca.
June (2018). J. Madariaga-Marcos talk (Best talk award!) and A. Marin-Gonzalez poster (Best poster award!) at SBE Conference, Castellon.
June (2018). J. Madariaga-Marcos talk and A. Martin-Gonzalez talk at 8th Workshop of Young Researchers in Nanoscience.
June (2018). We welcome Tung Le and Adam Jalal for a short visit to our lab.
May (2018). Toseland´s and Moreno´s lab meeting in Madrid. First meeting of the i-Link Project funded by CSIC.
May (2018). New paper published in Nucleic Acids Research on TubR–centromere complex.
May (2018). S. Hormeño talk at the B-6 Department Seminars, CNB, Madrid.
In prokaryotes, the centromere is a specialized segment of DNA that promotes the assembly of the segrosome upon binding of the Centromere Binding Protein (CBP). Here, we combine biochemical reconstruction and structural and biophysical analysis to bring light to the architecture of the segrosome complex in Type III partition systems.Continue Reading
Journal of Molecular Biology (2018). Volume 430, Issue 10, 11 May 2018, Pages 1495-1509. Available online 4 April 2018. https://doi.org/10.1016/j.jmb.2018.03.027
Pulmonary surfactant protein D (SP-D) is a glycoprotein from the collectin family that is a component of the lung surfactant system. It exhibits host defense and immune regulatory functions in addition to contributing to the homeostasis of the surfactant pool within the alveolar airspaces. It is known that the SP-D monomer forms trimers, which further associate into higher-order oligomers. However, the pathway and the interactions involved in the assembly of SP-D oligomers are not clearly understood. In the current study, a recombinant form of full-length human SP-D (rhSP-D) has been qualitatively and quantitatively studied by atomic force microscopy (AFM) and electrophoresis, with the aim to understand the conformational diversity and the determinants defining the oligomerization of the protein. The rhSP-D preparation studied is a mixture of trimers, hexamers, dodecamers and higher-order oligomeric species, with dodecamers accounting for more than 50% of the protein by mass. Similar structures were also found in hSP-D obtained from proteinosis patients, with the largest fuzzy-ball-like oligomers being more abundant in these samples. The proportion of dodecamer is increased under acidic conditions, accompanied by a conformational change into more compact configurations. Two hexamers appear to be the minimal necessary unit for dodecamer formation, with stabilization of the dodecamer occurring via non-covalent, ionic, and hydrophobic interactions between the individual N-terminal domains and the proximal area of the SP-D collagen stems.
Combining single-molecule techniques with fluorescence microscopy has attracted much interest because it allows the correlation of mechanical measurements with directly visualized DNA : protein interactions. In particular, its combination with total internal reflection fluorescence microscopy (TIRF) is advantageous because of the high signal-to-noise ratio this technique achieves.Continue Reading
The ParB protein forms DNA bridging interactions around parS to condense DNA and earmark the bacterial chromosome for segregation. The molecular mechanism underlying the formation of these ParB networks is unclear. We show here that while the central DNA binding domain is essential for anchoring at parS, this interaction is not required for DNA condensation.Continue Reading
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