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The ubiquitin-proteasome (Ub-Pr) degradation pathway regulates many cellular activities, but how ubiquitinated substrates are targeted to the proteasome is not understood. We have shown previously that valosin-containing protein (VCP) physically and functionally targets the ubiquitinated nuclear factor kappaB inhibitor, IkappaBalpha to the proteasome for(More)
The inactivation of the prototype NF-kappaB inhibitor, IkappaBalpha, occurs through a series of ordered processes including phosphorylation, ubiquitin conjugation, and proteasome-mediated degradation. We identify valosin-containing protein (VCP), an AAA (ATPases associated with a variety of cellular activities) family member, that co-precipitates with(More)
We have previously shown that NF-kappa B/Rel family members are physically associated phosphoproteins, and p105 and p50 are hyperphosphorylated after NF-kappa B activation. In this report, we further studied the phosphorylation involved in NF-kappa B activation in Jurkat T cells responding to phorbol 12-myristate 13-acetate and phytohemagglutinin.(More)
In most cells, the inactive dimeric NF-kappa B complexes are retained in the cytoplasm by binding to a group of inhibitory proteins. I kappa B. In response to extracellular stimuli, I kappa B is rapidly phosphorylated and degraded, thus, liberating the active NF-kappa B. To investigate the mechanisms involved, we have developed a cell-free system to study(More)
The ubiquitin-dependent proteasome-mediated (Ub-Pr) degradation pathway has been shown to regulate a large variety of substrates, including nuclear, cytosolic, and membrane proteins. In mammalian systems, polyubiquitin modification has been identified in a number of cell surface receptors for more than a decade; however, its biological significance has(More)
We performed radioimmunoprecipitation followed by serial immunoblots to show that, in the unstimulated Jurkat T cell line, the NF-kappa B/Rel family proteins, p80-c-Rel, p105-NF-kappa B, p65-NF-kappa B, p50-NF-kappa B and p36-I kappa B alpha, can be detected as complexes using antisera against c-Rel, p105-NF-kappa B or p65-NF-kappa B. p36-I kappa B alpha(More)
Mutation pgsA affecting the phosphatidylglycerol phosphate synthesis is lethal for all but certain E. coli strains such as strains deleted for the lpp gene or strains containing unmodifiable prolipoprotein like lppD14. Strain SD312 pgsA3 is tolerant to pgsA mutation, which suggests the lpp alleles in strain SD312 pgsA3 and its parental strain SD12 may be(More)
The particles of CPV of silkworm contain double-stranded RNA polymerase and methyltransferase. It was reported in a previous paper that the genome-enzyme complex could be isolated. The genome-enzyme complex shows high enzyme activity of RNA polymerase and methyltransferase in spite of the fact that it consists of only 5 percent of the protein. In order to(More)
The genome-enzyme complex is isolated from the silkworm cytoplasmic polyhedrosis virus with DEAE-Sephadex column chromatography after ultraviolet irradiation. The genome-enzyme complex shows both RNA-polymerase and methyltransferase activities while using 3H-UTP and [3H-methyl]-S-adenosyle-L-methionine as substrates. Like the double-stranded RNA genome of(More)
The coding properties of each mRNA synthesized in vitro of CPV have been examined. The mRNAs were separated by polyacrylamide gel electrophoresis and isolated from the gel slices. The individual mRNA was then translated into the wheat germ cell-free protein synthesizing system. The products of translation were analyzed by the immuno-reaction with the(More)