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  • Journal article

  • The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

    • Authors : Knoke, Lisa R. (2023)

  • The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative 14 power and the DsbC/D system as its complement for isomerization of non-native disulfides. 15 While the standard redox potentials of those systems are known, the in vivo redox potential 16 imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used 17 genetically encoded redox probes (roGFP2 ...
  • Journal article

  • Chemical Proteomics Reveals Protein Tyrosination Extends Beyond the Alpha-Tubulins in Human Cells

    • Authors : Makarov, Dmytro  (2023)

  • Tubulin detyrosination-tyrosination cycle regulates the stability of microtubules. Thus far described on α-tubulins, the tyrosination level is maintained by a single tubulin-tyrosine ligase (TTL). However, the precise dynamics and tubulin isoforms which undergo (de)tyrosination in neurons are unknown. Here, we exploit the substrate promiscuity of the TTL to introduce an O-propargyl-L-tyrosine in neuroblastoma cells and neurons. Mass spectrometry-based chemical proteomics in neuroblas...
  • Journal article

  • Coenzyme A binding sites induce proximal acylation across protein families

    • Authors : Carrico, Chris (2023)

  • Lysine Nɛ-acylations, such as acetylation or succinylation, are post-translational modifications that regulate protein function. In mitochondria, lysine acylation is predominantly non-enzymatic, and only a specific subset of the proteome is acylated. Coenzyme A (CoA) can act as an acyl group carrier via a thioester bond, but what controls the acylation of mitochondrial lysines remains poorly understood. Using published datasets, here we found that pr...
  • Journal article

  • A conformational-dependent interdomain redox relay at the core of Protein Disulfide Isomerase activity

    • Authors : Melo, Eduardo P. (2023)

  • Protein disulfide isomerases (PDIs) are a family of molecular chaperones resident in the endoplasmic reticulum (ER) emerging as important factors in disease. In addition to an holdase function, some members catalyse disulfide bond formation and isomerization, a crucial step for native folding and prevention of aggregation of misfolded proteins. PDIs are characterized by a modular arrangement of thioredoxin-like domains, with the canonical, first identified PDIA1, ...
  • Journal article

  • Phase Separation and Ageing of Glycine-Rich Protein from Tick Adhesive

    • Authors : Ganar, Ketan A. (2023)

  • Hard ticks feed on their host for multiple days. To ensure firm attachment, they secrete a protein-rich saliva that eventually forms a solid cement cone. The underlying mechanism of this liquid-to-solid transition is not yet understood. This study focuses on the phase transitions of a disordered glycine- rich protein (GRP) that is prominent in tick saliva. We show that GRP undergoes liquid-liquid phase separation via simple coacervatio...
  • Journal article

  • The cardiac myosin binding protein-C phosphorylation state as a function of multiple protein kinase and phosphatase activities

    • Authors : Kampourakis, Thomas (2023)

  • Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) is a crucial determinant of cardiac myofilament function. Although cMyBP-C phosphorylation by various protein kinases has been extensively studied, the influence of protein phosphatases on cMyBP-C’s multiple phosphorylation sites has remained largely obscure. Here we provide a detailed biochemical characterization of cMyBP-C dephosphorylation by protein phosphatases 1 and 2A (PP1 and PP2A) and deve...