Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.64 (proteinase K)
 4,071 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An activity that inhibits deoxyuridine triphosphatase (dUTPase) has been partially purified from Drosophila melanogaster. The inhibitor has a sedimentation coefficient of 4.1 S and a subunit molecular mass of 61 kDa. Its expression is limited to early stages of development, similar to the pattern previously found for dUTPase. The inhibitor is unusually stable to heating and is insensitive to DNAse and RNAse treatment. On the other hand, inhibition is sensitive to digestion with proteinase K, indicating that a protein is required for activity. These results suggest that at least one form of regulation is exerted on Drosophila dUTPase that could allow a greater opportunity for the incorporation of uracil into DNA.
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PMID:Control of Drosophila deoxyuridine triphosphatase. Existence of a developmentally expressed protein inhibitor. 254 93

Pseudorabies virus (PRV), a member of the Alphaherpesvirinae, has a complex multilayered extracellular virion that is structurally conserved among other herpesviruses. PRV virions contain a double-stranded DNA genome within a proteinaceous capsid surrounded by the tegument, a layer of viral and cellular proteins. The envelope layer, which encloses the capsid and tegument, contains viral transmembrane proteins anchored in a phospholipid bilayer. The viral and host proteins contained within virions execute important functions during viral spread and pathogenesis, but a detailed understanding of the composition of PRV virions has been lacking. In this report, we present the first comprehensive proteomic characterization of purified PRV virions by mass spectrometry using two complementary approaches. To exclude proteins present in the extracellular medium that may nonspecifically associate with virions, we also analyzed virions treated with proteinase K and samples prepared from mock-infected cells. Overall, we identified 47 viral proteins associated with PRV virions, 40 of which were previously localized to the capsid, tegument, and envelope layers using traditional biochemical approaches. Additionally, we identified seven viral proteins that were previously undetected in virions, including pUL8, pUL20, pUL32, pUL40 (RR2), pUL42, pUL50 (dUTPase), and Rsp40/ICP22. Furthermore, although we did not enrich for posttranslational modifications, we detected phosphorylation of four virion proteins: pUL26, pUL36, pUL46, and pUL48. Finally, we identified 48 host proteins associated with PRV virions, many of which have known functions in important cellular pathways such as intracellular signaling, mRNA translation and processing, cytoskeletal dynamics, and membrane organization. This analysis extends previous work aimed at determining the composition of herpesvirus virions and provides novel insights critical for understanding the mechanisms underlying PRV entry, assembly, egress, spread, and pathogenesis.
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PMID:Proteomic characterization of pseudorabies virus extracellular virions. 2152 50