Publications by authors named "D Podlesainski"
Article Synopsis
- Photosynthetic organisms like cyanobacteria adjust their carbohydrate metabolism based on light conditions, switching between making and breaking down carbohydrates.
- A study on the cyanobacterium Synechocystis sp. PCC 6803 revealed two iso-enzymes of phosphofructokinase (PFK) that uniquely use ADP instead of ATP and have different regulatory mechanisms affecting their activity in light and darkness.
- This finding is significant as it shows a previously undocumented ADP dependence in the PFK-A enzyme family, suggesting a unique evolutionary adaptation in some cyanobacteria and a few related bacteria.
Within the cell, chemical reactions are often confined and organized through a modular architecture. This facilitates the targeted localization of molecular species and their efficient translocation to subsequent sites. Here we present a cell-free nanoscale model that exploits compartmentalization strategies to carry out regulated protein unfolding and degradation.
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- Loss-of-function mutations in the HTRA1 protein lead to cerebral vasculopathy, a condition that affects brain blood vessels.
- The study identifies an HTRA1 variant that effectively corrects trimer assembly defects, restoring its enzymatic function, as well as a peptidic ligand that activates HTRA1 monomers.
- Findings suggest potential strategies for targeted protein repair, offering hope for therapeutic approaches to conditions related to HTRA1 mutations.
Article Synopsis
- The growing issue of antimicrobial resistance highlights the urgent need for new treatments against Mycobacterium tuberculosis (Mtb), leading researchers to explore callyaerins, a class of unique hydrophobic cyclopeptides, as potential anti-tubercular agents.
- Callyaerins are effective against various strains of Mtb, including those resistant to existing antibiotics, showing minimal harm to human cells and strong intracellular activity.
- Studies reveal that callyaerins target a specific membrane protein in Mtb, Rv2113, causing significant disturbances in vital cellular processes like lipid synthesis and DNA repair, indicating that even non-essential proteins could be promising targets for new antimycobacterial drugs.
The ClpC1:ClpP1P2 protease is a core component of the proteostasis system in mycobacteria. To improve the efficacy of antitubercular agents targeting the Clp protease, we characterized the mechanism of the antibiotics cyclomarin A and ecumicin. Quantitative proteomics revealed that the antibiotics cause massive proteome imbalances, including upregulation of two unannotated yet conserved stress response factors, ClpC2 and ClpC3.
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