title: The interactions of the largest subunit of RNA polymerase II with other cellular proteins: a bioinformatic approach.
abstract: The function of a protein is governed by its interaction with other proteins inside a cell. Therefore, it is important to identify the interacting partners of a particular protein to decipher its function. The protein interaction networks are generally determined by bioinformatic as well as experimental methodologies such as yeast two hybrid, mass spectrometry, immunoprecipitation, and fluorescence resonance energy transfer assays. Here, we have analyzed bioinformatically the interactions of Rpb1p (the largest subunit of RNA Polymerase II) with other proteins in yeast, using Cytoscape software and Biogrid/Biomart database. We find that Rpb1p interacts with a large number of proteins involved in mRNA synthesis, processing, export, and other cellular processes. These results validate the application of such bioinformatic approach to determine the interactome for other cellular proteins.
authors.affiliation: Southern Illinois University School of Medicine, Department of Biochemistry and Molecular Biology, Carbondale, IL 62901, USA.
authors.forename: Abhijit
authors.initials: A
authors.lastname: Shukla
authors.forename: Aparna
authors.initials: A
authors.lastname: Natarajan
authors.forename: Sukesh
authors.initials: S
authors.lastname: Bhaumik
authors.forename: Hany A
authors.initials: HA
authors.lastname: El-Shemy
authors.forename: David
authors.initials: D
authors.lastname: Lightfoot
mesh_terms: D011485:Protein Binding; D025941:Protein Interaction Mapping; D012319:RNA Polymerase II / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D012319:RNA Polymerase II; C511736:RPB1 protein, S cerevisiae