Cryo‐EM structure of the chain‐elongating E3 ubiquitin ligase UBR5
Z Hodáková, I Grishkovskaya, HL Brunner… - The EMBO …, 2023 - embopress.org
UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …
Recognition of the TDP-43 nuclear localization signal by importin α1/β
Cytoplasmic mislocalization of the TAR-DNA binding protein of 43 kDa (TDP-43) leads to
large, insoluble aggregates that are a hallmark of amyotrophic lateral sclerosis and …
large, insoluble aggregates that are a hallmark of amyotrophic lateral sclerosis and …
The world of stable ribonucleoproteins and its mapping with Grad-seq and related approaches
Macromolecular complexes of proteins and RNAs are essential building blocks of cells.
These stable supramolecular particles can be viewed as minimal biochemical units whose …
These stable supramolecular particles can be viewed as minimal biochemical units whose …
Structure of the human UBR5 E3 ubiquitin ligase
The human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …
Outer membrane protein evolution
R Dhar, JSG Slusky - Current opinion in structural biology, 2021 - Elsevier
Highlights•Most OMBBs evolved from an ancestral β-hairpin structure through a distinct
divergent evolutionary pathway.•Eukaryotic OMBBs evolved from that same l β-hairpin, but …
divergent evolutionary pathway.•Eukaryotic OMBBs evolved from that same l β-hairpin, but …
Creative destruction: New protein folds from old
C Alvarez-Carreño, RJ Gupta… - Proceedings of the …, 2022 - National Acad Sciences
Mechanisms of emergence and divergence of protein folds pose central questions in
biological sciences. Incremental mutation and stepwise adaptation explain relationships …
biological sciences. Incremental mutation and stepwise adaptation explain relationships …
A widespread family of WYL-domain transcriptional regulators co-localizes with diverse phage defence systems and islands
DM Picton, JD Harling-Lee, SJ Duffner… - Nucleic Acids …, 2022 - academic.oup.com
Bacteria are under constant assault by bacteriophages and other mobile genetic elements.
As a result, bacteria have evolved a multitude of systems that protect from attack. Genes …
As a result, bacteria have evolved a multitude of systems that protect from attack. Genes …
Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways
Rossmann folds are ancient, frequently diverged domains found in many biological reaction
pathways where they have adapted for different functions. Consequently, discernment and …
pathways where they have adapted for different functions. Consequently, discernment and …
Fold evolution before LUCA: common ancestry of SH3 domains and OB domains
SH3 and OB are the simplest, oldest, and most common protein domains within the
translation system. SH3 and OB domains are β-barrels that are structurally similar but are …
translation system. SH3 and OB domains are β-barrels that are structurally similar but are …
Characterization of a fold in TANGO1 evolved from SH3 domains for the export of bulky cargos
O Arnolds, R Stoll - Nature Communications, 2023 - nature.com
Bulky cargos like procollagens, apolipoproteins, and mucins exceed the size of conventional
COPII vesicles. During evolution a process emerged in metazoans, predominantly governed …
COPII vesicles. During evolution a process emerged in metazoans, predominantly governed …