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PubMedDate not supplied

Evolution in bioids: hypercompetitivity as a source of bistability and a possible role of metal complexes as prenucleoprotic mediators of molecular asymmetry.

Spontaneous production of optically active compounds can occur through kinetic instability of an asymmetric steady state in open systems, in which two enantiomeric autocatalysts compete for a common prochiral substrate in a stereoselective reaction of order n greater than 2. For the case of n=3, a proof of instability of a symmetric reacting state in the general case, and functions of reaction parameters ('Chemical Reynolds Numbers') governing the existence and stability of 7 different steady states are derived. The 'extinct state' (without autocatalyst) is stable; a finite amount of products is required to shift it into one of the reacting steady states. A mutation from one state into another in such system ('bioids') involves an amplification of different 'kinds of information', as 'stochastic' (noise into dissipative structures), 'molecular' (autocatalysts), and 'stoichimetric' information. Stereospecific third order kinetics are believed to be realizable on octahedral metal complexes with two-dentated ligands and to have played a role in the prebiological evolution of optically active compounds.

Biological Evolution↗
PubMed2026

Comprehensive proximity proteomics expand the known interactome of the oncoprotein β-catenin.

The oncoprotein β-catenin has critical roles in cell adhesion and cell signalling. β-catenin affects human physiology and pathology through numerous interaction partners, of which many have been discovered by standard affinity purification-based proteomics. However, the interaction landscape of β-catenin remains incompletely understood, highlighting a need for new experimental approaches for the exploration of β-catenin biology. Proximity proteomics, which facilitate the discovery of molecules vicinal to proteins-of-interest by mass spectrometry, have recently emerged as a powerful complementary tool for the study of protein-protein interactions, but have not been applied to β-catenin so far. We investigated the interactome of β-catenin in model cell lines by proximity proteomics using expression constructs with the biotin ligases BioID and TurboID. Mass spectrometry analyses following biotin labelling identified numerous candidate interactors of β-catenin, including many that had not been observed in earlier studies using standard proteomics. Enrichment analyses suggested that proximity proteomics capture proteins associated with the known biological functions of β-catenin, including cell adhesion, Wnt/β-catenin signalling, and transcription regulation. The molecular tools and data generated in this study provide new insights into β-catenin biology and highlight potential new regulators of β-catenin function that warrant further exploration.

beta Catenin↗
PubMed2024

MX2 forms nucleoporin-comprising cytoplasmic biomolecular condensates that lure viral capsids.

Human myxovirus resistance 2 (MX2) can restrict HIV-1 and herpesviruses at a post-entry step through a process requiring an interaction between MX2 and the viral capsids. The involvement of other host cell factors, however, remains poorly understood. Here, we mapped the proximity interactome of MX2, revealing strong enrichment of phenylalanine-glycine (FG)-rich proteins related to the nuclear pore complex as well as proteins that are part of cytoplasmic ribonucleoprotein granules. MX2 interacted with these proteins to form multiprotein cytoplasmic biomolecular condensates that were essential for its anti-HIV-1 and anti-herpes simplex virus 1 (HSV-1) activity. MX2 condensate formation required the disordered N-terminal region and MX2 dimerization. Incoming HIV-1 and HSV-1 capsids associated with MX2 at these dynamic cytoplasmic biomolecular condensates, preventing nuclear entry of their viral genomes. Thus, MX2 forms cytoplasmic condensates that likely act as nuclear pore decoys, trapping capsids and inducing premature viral genome release to interfere with nuclear targeting of HIV-1 and HSV-1.

Humans↗