The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation

Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5′-AMP; second, the biotinyl moiety is ligated to lysine residues. It has been proposed that step two is fairly promiscuous, and that protein biotinylation may occur in the absence of HCS as long as sufficient exogenous biotinyl-5′- AMP is provided. Here, we identified a novel polypeptide (Syn67) with a basic patch of lysines and arginines. Yeast-two-hybrid assays and limited proteolysis assays revealed that both N- and C-termini of HCS interact with Syn67. A potential target lysine in Syn67 was biotinylated by HCS only after arginine-to-glycine substitutions in Syn67 produced a histone-like peptide. We identified a Syn67 docking site near the active pocket of HCS by in silico modeling and site directed mutagenesis. Biotinylation of proteins by HCS is more specific than previously assumed

The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation

Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5′-AMP; second, the biotinyl moiety is ligated to lysine residues. It has been proposed that step two is fairly promiscuous, and that protein biotinylation may occur in the absence of HCS as long as sufficient exogenous biotinyl-5′- AMP is provided. Here, we identified a novel polypeptide (Syn67) with a basic patch of lysines and arginines. Yeast-two-hybrid assays and limited proteolysis assays revealed that both N- and C-termini of HCS interact with Syn67. A potential target lysine in Syn67 was biotinylated by HCS only after arginine-to-glycine substitutions in Syn67 produced a histone-like peptide. We identified a Syn67 docking site near the active pocket of HCS by in silico modeling and site directed mutagenesis. Biotinylation of proteins by HCS is more specific than previously assumed

Holocarboxylasesynthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events

Holocarboxylasesynthetase (HCS) catalyzes the binding of the vitamin biotin to histonesH3 and H4, thereby creating rare histonebiotinylation marks in the epigenome. These marksco-localize with K9-methylated histone H3 (H3K9me), an abundant gene repression mark. The abundance of H3K9me marks in transcriptionally competent loci decreases when HCS is knocked down and when cells are depleted of biotin. Here we tested the hypothesis that the creation of H3K9me marks is at least partially explained by physical interactions between HCS and histone-lysine Nmethyltransferases. Using a novel in silico protocol, we predicted that HCS-interacting proteins contain a GGGG(K/R)G(I/M)R motif. Thismotif, with minor variations, is present in the histonelysine N-methyltransferase EHMT1. Physical interactions between HCS and the N-terminal, ankyrin, and SET domains in EHMT1 were confirmed using yeast-two-hybrid assays, limited proteolysis assays, and co-immunoprecipitation. The interactions were stronger between HCS and the N-terminus in EHMT1 compared with the ankyrin and SET domains, consistent with the localization of the HCS-binding motif in the EHMT1 N-terminus. HCS has the catalytic activity to biotinylate K161 within the binding motif in EHMT1. Mutation of K161 weakenedthe physical interaction between EHMT1 and HCS, but it is unknown whether this effect was caused by loss of biotinylation or loss of the motif. Importantly, HCS knockdown decreased the abundance of H3K9me marks in repeats, suggesting that HCS plays a role in creating histone methylation marks in these loci. We conclude that physical interactionsbetween HCS and EHMT1 mediate epigenomic synergies between biotinylation and methylation events

ICTV Virus Taxonomy Profile: Chrysoviridae

The Chrysoviridae is a family of small, isometric, non-enveloped viruses (40 nm in diameter) with segmented dsRNA genomes (typically four segments). The genome segments are individually encapsidated and together comprise 11.5–12.8 kbp. The single genus Chrysovirus includes nine species. Chrysoviruses lack an extracellular phase to their life cycle; they are transmitted via intracellular routes within an individual during hyphal growth, in asexual or sexual spores, or between individuals via hyphal anastomosis. There are no known natural vectors for chrysoviruses. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the taxonomy of the Chrysoviridae, which is available at www.ictv.global/report/chrysoviridae.Peer reviewe

ICTV Virus Taxonomy Profile: Chrysoviridae

Members of the family Chrysoviridae are isometric, non-enveloped viruses with segmented, linear, dsRNA genomes. There are 3–7 genomic segments, each of which is individually encapsidated. Chrysoviruses infect fungi, plants and possibly insects, and may cause hypovirulence in their fungal hosts. Chrysoviruses have no known vectors and lack an extracellular phase to their replication cycle; they are transmitted via intracellular routes within an individual during hyphal growth, in asexual or sexual spores, or between individuals via hyphal anastomosis. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the taxonomy of the family Chrysoviridae, which is available at ictv.global/report/chrysoviridae.Peer reviewe

Evidence for directed percolation universality at the onset of spatiotemporal intermittency in coupled circle maps

We consider a lattice of coupled circle maps, a model arising naturally in descriptions of solid state phenomena such as Josephson junction arrays. We find that the onset of spatiotemporal intermittency (STI) in this system is analogous to directed percolation (DP), with the transition being to an unique absorbing state for low nonlinearities, and to weakly chaotic absorbing states for high nonlinearities. We find that the complete set of static exponents and spreading exponents at all critical points match those of DP very convincingly. Further, hyperscaling relations are fulfilled, leading to independent controls and consistency checks of the values of all the critical exponents. These results lend strong support to the conjecture that the onset of STI in deterministic models belongs to the DP universality class.Comment: Submitted to Physical Review

Coulomb correlations effects on localized charge relaxation in the coupled quantum dots

We analyzed localized charge time evolution in the system of two interacting quantum dots (QD) (artificial molecule) coupled with the continuous spectrum states. We demonstrated that Coulomb interaction modifies relaxation rates and is responsible for non-monotonic time evolution of the localized charge. We suggested new mechanism of this non-monotonic charge time evolution connected with charge redistribution between different relaxation channels in each QD.Comment: 10 pages, 10 figure

Search for solar axions using Li-7

We describe a novel approach to the search for solar, near-monochromatic hadronic axions, the latter being suggested to be created in the solar core during M1 transitions between the first excited level of Li-7, at 478 keV, and the ground state. As a result of Doppler broadening, in principle these axions can be detected via resonant absorption by the same nuclide on the Earth. Excited nuclei of Li-7 are produced in the solar interior by Be-7 electron capture and thus the axions are accompanied by emission of Be-7 solar neutrinos of energy 384 keV. An experiment was made which has yielded an upper limit on hadronic axion mass of 32 keV at the 95% confidence level.Comment: revtex, 4 pages with 2 figures, title revised, minor changes, matches version to appear in Phys. Rev.

Severe Acute Respiratory Syndrome Coronavirus Viroporin 3a Activates the NLRP3 Inflammasome

Nod-like receptor family, pyrin domain-containing 3 (NLRP3) regulates the secretion of proinflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. We previously showed that influenza virus M2 or encephalomyocarditis virus (EMCV) 2B proteins stimulate IL-1β secretion following activation of the NLRP3 inflammasome. However, the mechanism by which severe acute respiratory syndrome coronavirus (SARS-CoV) activates the NLRP3 inflammasome remains unknown. Here, we provide direct evidence that SARS-CoV 3a protein activates the NLRP3 inflammasome in lipopolysaccharide-primed macrophages. SARS-CoV 3a was sufficient to cause the NLRP3 inflammasome activation. The ion channel activity of the 3a protein was essential for 3a-mediated IL-1β secretion. While cells uninfected or infected with a lentivirus expressing a 3a protein defective in ion channel activity expressed NLRP3 uniformly throughout the cytoplasm, NLRP3 was redistributed to the perinuclear space in cells infected with a lentivirus expressing the 3a protein. K+ efflux and mitochondrial reactive oxygen species were important for SARS-CoV 3a-induced NLRP3 inflammasome activation. These results highlight the importance of viroporins, transmembrane pore-forming viral proteins, in virus-induced NLRP3 inflammasome activation