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P105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells.

ABSTRACT: Active NF-kappa B-like transcription complexes are multimers consisting of one or two members of a family of proteins related to the c-Rel proto-oncoprotein. We have isolated a chicken cDNA encoding p105, the precursor protein for the p50 subunit of NF-kappa B. Sequence analysis shows that chicken p105 is approximately 70% identical to the mouse and human p105 proteins, containing the Rel homology domain in its N-terminal 370 amino acids and several ankyrinlike repeats in the C-terminal portion of the protein. The Rel homology domain is particularly highly conserved between chicken and mammalian p50, and an in vitro-synthesized, truncated chicken p105 protein, containing sequences that correspond to the predicted p50 protein, bound to a consensus kappa B site in an electrophoretic mobility shift assay. In v-Rel-transformed chicken spleen cells, v-Rel is found in high-molecular-weight complexes which include cellular proteins of approximately 124 kDa (p124) and 115 kDa (p115). Here we report that in vitro-produced p105 comigrates with p124 from v-Rel-transformed spleen cells and that p105 and p124 appear to be identical by partial proteolytic mapping with V8 protease. Furthermore, both p105 and p50 can complex directly with v-Rel and chicken c-Rel in vitro. However, in vitro association with p105 by v-Rel does not necessarily correlate with transformation, since one nontransforming v-Rel mutant can associate with p105 in vitro.

SUBMITTER: Capobianco AJ

PROVIDER: S-EPMC241161 | biostudies-other | 1992 Jun

REPOSITORIES: biostudies-other

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p105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells.

Capobianco A J AJ Chang D D Mosialos G G Gilmore T D TD

Journal of virology 19920601 6

Active NF-kappa B-like transcription complexes are multimers consisting of one or two members of a family of proteins related to the c-Rel proto-oncoprotein. We have isolated a chicken cDNA encoding p105, the precursor protein for the p50 subunit of NF-kappa B. Sequence analysis shows that chicken p105 is approximately 70% identical to the mouse and human p105 proteins, containing the Rel homology domain in its N-terminal 370 amino acids and several ankyrinlike repeats in the C-terminal portion ...[more]

PMID: 1533881

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Project description:BackgroundDietary phytochemicals consist of a wide variety of biologically active compounds that are ubiquitous in plants, many of which have been reported to have anti-tumor as well as anti-inflammatory properties.ObjectiveIn the present study, we aimed to validate these findings by using docking protocols and explicate the possible mechanism of action for a dataset of nine phytochemicals namely boswellic acid, 1-caffeoylquinic acid, ellagic acid, emodin, genistein, guggulsterone, quercetin, resveratrol, and sylibinin from different plants against the nuclear factor- kappaB (NF-κB) precursor protein p105, an important transcription factor reported to be overexpressed in breast cancer.Materials and methods2-D structures of all phytochemicals were retrieved from PubChem Compound database and their subsequent conversion into 3-D structures was performed by using online software system CORINA. The X-ray crystallographic structure of the NF-κB precursor p105 was extracted from Brookhaven Protein Data Bank. Molecular docking simulation study was carried out by using AutoDock Tools 4.0.ResultsOur results showed significant binding affinity of different phytochemicals with the Rel homology domain of the NF-κB precursor protein p105. Quercetin and 1-caffeoylquinic acid were found to be very effective inhibitors against target molecule as they showed binding energy of -12.11 and -11.50 Kcal/mol, respectively. The order of affinity of other ligands with p105 was found as follows: guggulsterone > sylibinin > emodin > resveratrol > genistein > boswellic acid > ellagic acid.ConclusionOur in silico study has explored the possible chemopreventive mechanism of these phytochemicals against the NF-κB precursor protein p105 and deciphered that quercetin, 1-caffeoylquinic acid and guggulsterone were the potent inhibitors against target molecule. In addition, large scale preclinical and clinical trials are needed to explore the role of these chemotherapeutic molecules against the NF-κB precursor protein p105 in cure and prevention of breast cancer.

Dataset Information

P105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells.

Publications

p105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells.

Similar Datasets

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