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Full-Text Articles in Molecular Biology
A Drosophila Protein-Interaction Map Centered On Cell-Cycle Regulators, Clement A. Stanyon, Guozhen Liu, Bernardo A. Mangiola, Nishi Patel, Loic Giot, Bing Kuang, Huamei Zhang, Jinhui Zhong, Russell L. Finley Jr
A Drosophila Protein-Interaction Map Centered On Cell-Cycle Regulators, Clement A. Stanyon, Guozhen Liu, Bernardo A. Mangiola, Nishi Patel, Loic Giot, Bing Kuang, Huamei Zhang, Jinhui Zhong, Russell L. Finley Jr
Wayne State University Associated BioMed Central Scholarship
Abstract
Background
Maps depicting binary interactions between proteins can be powerful starting points for understanding biological systems. A proven technology for generating such maps is high-throughput yeast two-hybrid screening. In the most extensive screen to date, a Gal4-based two-hybrid system was used recently to detect over 20,000 interactions among Drosophila proteins. Although these data are a valuable resource for insights into protein networks, they cover only a fraction of the expected number of interactions.
Results
To complement the Gal4-based interaction data, we used the same set of Drosophila open reading frames to construct arrays for a LexA-based two-hybrid system. We …
Integrated Allosteric Regulation In The S. Cerevisiae Carbamylphosphate Synthetase – Aspartate Transcarbamylase Multifunctional Protein, Valã©Rie Serre, Bernadette Penverne, Jean-Luc Souciet, Serge Potier, Hedeel Guy, David Evans, Patrick Vicart, Guy Hervã©
Integrated Allosteric Regulation In The S. Cerevisiae Carbamylphosphate Synthetase – Aspartate Transcarbamylase Multifunctional Protein, Valã©Rie Serre, Bernadette Penverne, Jean-Luc Souciet, Serge Potier, Hedeel Guy, David Evans, Patrick Vicart, Guy Hervã©
Wayne State University Associated BioMed Central Scholarship
Abstract
Background
The S. cerevisiae carbamylphosphate synthetase – aspartate transcarbamylase multifunctional protein catalyses the first two reactions of the pyrimidine pathway. In this organism, these two reactions are feedback inhibited by the end product UTP. In the present work, the mechanisms of these integrated inhibitions were studied.
Results
The results obtained show that the inhibition is competitive in the case of carbamylphosphate synthetase and non-competitive in the case of aspartate transcarbamylase. They also identify the substrate whose binding is altered by this nucleotide and the step of the carbamylphosphate synthetase reaction which is inhibited. Furthermore, the structure of the domains …