Disease relevance of USP39

• In a fractionated cell extract, only those fractions containing this 65K protein could reverse the inhibition of DNA-dependent RNA synthesis by the plus-strand vesicular stomatitis virus leader RNA or by homologous DNA [1].
• The 65K phosphoprotein is usually by far the most abundant structural component found in culture-grown purified virus particles [2].
• Human cytomegalovirus contains a phosphorylated matrix protein of 65,000 apparent molecular weight (65K phosphoprotein; pp65) and a related phosphoprotein of 71,000 molecular weight (pp71) [2].
• The 65K antigen is detected in Raji cells but not in three Epstein-Barr virus (-) human B cell lines [3].
• Translation of early RNA specific for the leftmost early region 1 of adenovirus type 5 DNA in a rabbit reticulocyte cell-free system resulted in the synthesis of proteins with the following molecular weights: 65,000 (65K), 54K, 42 to 34K, 29K, 25K, 19K, and 18K [4].

High impact information on USP39

• This line showed a specific proliferative response to PPD and to a recombinant mycobacterial heat-shock protein (HSP) of relative molecular mass 65,000 (65K) [5].
• The AChR from the electroplax of the ray Torpedo californica consists of five subunits present in a molar stoichiometry of alpha 2 beta gamma delta (refs 4-6); the apparent molecular weights of the alpha-, beta-, gamma- and delta-subunits are 40,000 (40K), 50K, 60K and 65K, respectively [6].
• We provide evidence that, in contrast to the previously published U12 snRNA secondary structure model, the 3' half of U12 forms an extended stem-loop with a highly conserved seven-nucleotide loop and that the latter serves as the 65K binding site [7].
• In earlier work, we showed that Sad1, the gene encoding the first committed enzyme in the avenacin pathway (beta-amyrin synthase), had arisen by duplication and divergence of a cycloartenol synthase-like gene [8].
• Significantly, the major tri-snRNP-specific proteins 65K and 110K, which are required for integration of the major tri-snRNP into the U2-dependent spliceosome, were among those proteins detected in the minor tri-snRNP, raising an interesting question as to how the specificity of addition of tri-snRNP to the corresponding spliceosome is maintained [9].

Chemical compound and disease context of USP39

• All four FcRs were reactive with a murine monoclonal antibody to herpes simplex virus glycoprotein E. Anti-HCMV antibodies markedly inhibited the binding of 125I-labelled human IgG Fc to the 130K and 50K species but inhibited to a lesser extent the binding to the 65K FcR [10].

Biological context of USP39

• In studies with synthetic oligodeoxynucleotides homologous to leader RNA sequences, only those oligonucleotides containing the inhibitory sequence were able to bind to a gradient fraction containing the 65K protein [1].
• Pulse-chase experiments and experiments with monensin as an inhibitor of glycosylation suggested that the 120K polypeptide was derived by glycosylation of the 118K polypeptide and that a 43K antigen was processed into the 64 to 65K glycoprotein [11].
• The identification of a 65K protein among products synthesized in vitro suggests that this protein may be identical to the 65K major T antigen present in adenovirus type 5-infected and -transformed cells, and this indicates that it is indeed encoded by the viral genome [4].

Anatomical context of USP39

• These 2 M. leprae antigens, 36K and 65K, thus seem to contain major T cell epitopes [12].
• In the cell body preparation, the intermediate filament antibody labeled, in order of their staining intensity, a 65K, 60K, 74K, and 180K protein [13].
• Immunoblot analysis of human sera from individuals seropositive for HCMV showed that the recombinant pp65 products were as antigenic as the native 65K phosphoprotein produced in HCMV-infected human embryonic fibroblasts [14].
• Antibody Lan3-8 reacts with neurons in the nerve cord and gut but with epithelial cells in the penis; it binds to a 65K molecule in all three tissues [15].
• Both gH and gL were transcribed and translated in vitro to give products of apparent M(r) of 65K and 28K in SDS-PAGE, and these could be processed by addition of microsomes to 110K and 40K, respectively [16].

Associations of USP39 with chemical compounds

• A protein fraction, 65K, poorly-glycosylated, with high contents of Asx, Glx, and Gly was found strongly associated with both ROM and PSM, and was only separable by ultracentrifugation in 4M guanidine HCl and CsCl [17].
• A less prominent 65K mol. wt glycoprotein was also precipitated by AT72 from thymus and T cells but not from leukaemic T cells [18].
• Single crystals of guanine hydrochloride dihydrate, in which the guanine base is protonated at N7, were X-irradiated at 20K, 65K and 150K [19].
• Film thicknesses of 45, 80, and 100 nm were studied, using PS molecular weights ranging from 65K to 11.4 Mg/mol [20].
• Glucosamine labelled major glycoproteins migrated at 130K, 100K, 95K, 65K, 39K; mannose moieties migrated at 95K and 65K [21].

Analytical, diagnostic and therapeutic context of USP39

• The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay [22].
• Finally, the partially purified 65K antigen is an effective absorbant of EBNA antibody as measured in an anticomplement immunofluorescence assay [3].
• In SDS-PAGE, the purified Co-eIF-2C preparation and an eIF-3 preparation (purified in Dr. A. Wahba's laboratory) separated into seven similar major polypeptides (Mr 110K, 65K, 63K, 53K, 50K, 43K, and 40K) [23].
• The M. leprae-specific epitopes on the 36K and 65K antigen may help in the development of a specific serodiagnostic and skin test [12].
• Immunoprecipitation with extracts from infected cells revealed that the antibody recognized four glycosylated proteins (gps) with Mrs of 106K, 102K, 65K and 63K under reducing conditions [24].

References