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Here we investigated the expression of Apolipoprotein B mRNA-editing enzyme catalytic subunit 3G in feline cells and tissues, as well as whether its presence antagonizes the viral pre-integration complex that results in partial or complete FIV latency. To measure fA3G-like protein in cats exposed to elevated versus low-dose cell-associated FIV, real-time RT-PCR and western blot assays were used. We consistently detected fA3G-like protein in mock T-cell lines and primary bone marrow-derived macrophages with variable expressions in feline peripheral blood mononuclear cells. However, in lytic FIV infection, the fA3G-like protein decreased in early post-infection, but latently infected cats maintained stable expression. These results are the first reports of the fA3G-like protein expression in felines and its abrogation in lytic, but not in latent FIV-infected individuals. These results may help clarify the role of fA3G-like protein in the host defense system against retrovirus infections.
Source link: https://europepmc.org/article/PPR/PPR540089
Prokaryotes use cytochrome bd oxidases, which also play a key role in bacterial virulence and antibiotic resistance, among other enzymes. Here, we combine bioinformatics, mutagenesis, enzyme kinetics, and FTIR spectroscopy to show that proton delivery to the active site contributes to the rate limiting steps in Cyt bd-I, which includes Asp58 of subunit CydB.
Source link: https://europepmc.org/article/MED/36029102
This paper discusses the effect of fission yeast PC4 phosphorylation on RNAPII transcription in a cell extract that closely matches the cellular context. The phosphorylation of fission yeast PC4 is highly phosphorylated by the catalytic subunit of CK2, according to us, while the regulatory subunit regulates the PC4 phosphorylation. The addition of Cka1 to an in vitro transcription assay will decrease the basal transcription from the Ad-MLP promoter, however, the addition of recombinant fission yeast PC4 or Ckb1 in a cell extract can stimulate basal transcription. Fission yeast PC4 is phosphorylated in a domain that has consensus phosphorylation sites for CK2, and two serine residues have been identified as phosphorylation essential for CK2 phosphorylation. Mutation of one of the serine residues in PC4 does not entirely eliminate the phosphorylation; however, when the two serine residues are mutated, CK2 is no longer able to phosphorylate PC4.
Source link: https://europepmc.org/article/MED/36012759
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