Interactions between the human RNA polymerase II subunits.
As an initial approach to characterizing the molecular structure of the human RNA polymerase II (hRPB), we systematically investigated the protein-protein contacts that the subunits of this enzyme may establish with each other. To this end, we applied a glutathione S-transferase-pulldown assay to extracts from Sf9 insect cells, which were ... coinfected with all possible combinations of recombinant baculoviruses expressing hRPB subunits, either as untagged polypeptides or as glutathione S-transferase fusion proteins. This is the first comprehensive study of interactions between eukaryotic RNA polymerase subunits; among the 116 combinations of hRPB subunits tested, 56 showed significant to strong interactions, whereas 60 were negative. Within the intricate network of interactions, subunits hRPB3 and hRPB5 play a central role in polymerase organization. These subunits, which are able to homodimerize and to interact, may constitute the nucleation center for polymerase assembly, by providing a large interface to most of the other subunits.
Mesh Terms:
Baculoviridae, Cloning, Molecular, Cysteine, Glutathione, Humans, Methionine, Models, Molecular, Molecular Sequence Data, Protein Conformation, RNA Polymerase II
Baculoviridae, Cloning, Molecular, Cysteine, Glutathione, Humans, Methionine, Models, Molecular, Molecular Sequence Data, Protein Conformation, RNA Polymerase II
J. Biol. Chem.
Date: Jul. 04, 1997
PubMed ID: 9201987
View in: Pubmed Google Scholar
Download Curated Data For This Publication
12001
Switch View:
- Interactions 56