RUVBL1–RUVBL2 AAA-ATPase: a versatile scaffold for multiple complexes and functions
Bibliographic review of the RUVBL1-RUVBL2 complexes recently published by the OLl-CNIO group.
Continue ReadingCharacterizing microfluidic approaches for a fast and efficient reagent exchange in single-molecule studies
New publication within the NanoBioCancer consortium by the FMH-CNB group led by Fernando Moreno Herrero.
Continue ReadingStructural basis of Focal Adhesion Kinase activationon lipid membranes
New publication by Óscar Llorca's group (OL-CNIO).
Continue ReadingBulk and single-molecule analysis of a bacterial DNA2-like helicase–nuclease reveals a single-stranded DNA looping motor
New publication by Fernando Moreno Herrero's group where they use magnetic forceps to study the mechanism by which helicase-nuclease Bad unwinds the DNA double helix.
Continue ReadingRPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes
Despite the current situation, scientific production has not been altered. We are happy to inform you of a new publication by Oscar Llorca's group.
Continue ReadingUnderstanding the paradoxical mechanical response of in-phase A-tracts at different force regimes
New publication of the group of the coordinator of the NanoBioCancer program, Fernando Moreno Herrero.
Continue ReadingModeling of a 14 kDa RUVBL2-Binding Domain with Medium Resolution Cryo-EM Density
Nueva publicación dentro del consorcio NanoBioCancer-CM por parte del grupo de Oscar Llorca.
Continue ReadingDouble-stranded RNA bending by AU-tract sequences
Alberto Marin-Gonzalez, Clara Aicart-Ramos, Mikel Marin-Baquero, Alejandro Martín-González, Maarit Suomalainen, Abhilash Kannan, J. G. Vilhena, Urs F. Greber, Fernando Moreno-Herrero and Rubén Pérez.
Abstract: Sequence-dependent structural deformations of the DNA double helix (dsDNA) have been extensively studied, where adenine tracts (A-tracts) provide a striking example for global bending in the molecule. In
contrast to dsDNA, much less is known about how the nucleotide sequence affects bending deformations of double-stranded RNA (dsRNA). Using all-atom microsecond long molecular dynamics simulations we found a sequence motif consisting of alternating adenines and uracils, or AU-tracts, that bend the dsRNA helix by locally compressing the major groove. We experimentally tested this prediction using atomic force microscopy (AFM) imaging of long dsRNA molecules containing phased AU-tracts. AFM images revealed a clear intrinsic bend in these AU-tracts molecules, as quantified by a significantly lower persistence length compared to dsRNA molecules of arbitrary sequence. The bent structure of AU-tracts here described might play a role in sequence-specific recognition of dsRNAs by dsRNA-interacting proteins or impact the folding of RNA into intricate tertiary and quaternary structures.
Link to the publication.
Architecture of the mycobacterial type VII secretion system
Publication in the prestigious magazine Nature by Oscar Llorca's group
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