Two-Hybrid System Techniques

Publication Title: 
Nature Cell Biology

Protein ubiquitylation is a key post-translational control mechanism contributing to different physiological processes, such as signal transduction and ageing. The size and linkage of a ubiquitin chain, which determines whether a substrate is efficiently targeted for proteasomal degradation, is determined by the interplay between ubiquitylation and deubiquitylation. A conserved factor that orchestrates distinct substrate-processing co-regulators in diverse species is the ubiquitin-selective chaperone CDC-48 (also known as p97).

Author(s): 
Kuhlbrodt, Kirsten
Janiesch, Philipp Christoph
Kevei, …va
Segref, Alexandra
Barikbin, Roja
Hoppe, Thorsten
Publication Title: 
Annual Review of Nutrition

Nutrigenomics refers to the complex effects of the nutritional environment on the genome, epigenome, and proteome of an organism. The diverse tissue- and organ-specific effects of diet include gene expression patterns, organization of the chromatin, and protein post-translational modifications. Long-term effects of diet range from obesity and associated diseases such as diabetes and cardiovascular disease to increased or decreased longevity.

Author(s): 
Ruden, Douglas M.
De Luca, Maria
Garfinkel, Mark D.
Bynum, Kerry L.
Lu, Xiangyi
Publication Title: 
Science (New York, N.Y.)

Huntington's disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. Transcriptional dysregulation has been implicated in HD pathogenesis. Here, we report that huntingtin interacts with the transcriptional activator Sp1 and coactivator TAFII130. Coexpression of Sp1 and TAFII130 in cultured striatal cells from wild-type and HD transgenic mice reverses the transcriptional inhibition of the dopamine D2 receptor gene caused by mutant huntingtin, as well as protects neurons from huntingtin-induced cellular toxicity.

Author(s): 
Dunah, Anthone W.
Jeong, Hyunkyung
Griffin, April
Kim, Yong-Man
Standaert, David G.
Hersch, Steven M.
Mouradian, M. Maral
Young, Anne B.
Tanese, Naoko
Krainc, Dimitri
Publication Title: 
Proceedings of the National Academy of Sciences of the United States of America

Huntington's disease (HD) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). Pathogenesis in HD seems to involve the formation of neuronal intranuclear inclusions and the abnormal regulation of transcription and signal transduction. To identify previously uncharacterized htt-interacting proteins in a simple model system, we used a yeast two-hybrid screen with a Caenorhabditis elegans activation domain library. We found a predicted SH3 domain protein (K08E3.3b) that interacts with N-terminal htt in two-hybrid tests.

Author(s): 
Holbert, Sébastien
Dedeoglu, Alpaslan
Humbert, Sandrine
Saudou, Frédéric
Ferrante, Robert J.
Neri, Christian
Publication Title: 
Biochemical and Biophysical Research Communications

c-JUN is a major component of heterodimer transcription factor AP-1 (Activator Protein-1) that activates gene transcription in cell proliferation, inflammation and stress responses. SIRT1 (Sirtuin 1) is a histone deacetylase that controls gene transcription through modification of chromatin structure. However, it is not clear if SIRT1 regulates c-JUN activity in the control of gene transcription. Here, we show that SIRT1 associated with c-JUN in co-immunoprecipitation of whole cell lysate, and inhibited the transcriptional activity of c-JUN in the mammalian two hybridization system.

Author(s): 
Gao, Zhanguo
Ye, Jianping
Publication Title: 
The Journal of Biological Chemistry

Our recent study has shown that betaA3-crystallin along with betaB1- and betaB2-crystallins were part of high molecular weight complex obtained from young, old, and cataractous lenses suggesting potential interactions between alpha- and beta-crystallins (Srivastava, O. P., Srivastava, K., and Chaves, J. M. (2008) Mol. Vis. 14, 1872-1885). To investigate this further, this study was carried out to determine the interaction sites of betaA3-crystallin with alphaA- and alphaB-crystallins.

Author(s): 
Gupta, Ratna
Srivastava, Om P.
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