HOMCOS: a server to predict interacting protein pairs and interacting sites by homology modeling of complex structures.

As protein-protein interactions are crucial in most biological processes, it is valuable to understand how and where protein pairs interact. We developed a web server HOMCOS (Homology Modeling of Complex Structure, http://biunit.naist.

Prediction of interacting proteins from homology-modeled complex structures using sequence and structure scores.

Protein-protein interactions support most biological processes, and it is important to find specifically interacting partner proteins among homologous proteins in order to elucidate cellular functions such as signal transduction systems. Various high-throughput experimental methods for identifying these interactions have been invented, and used to generate a huge amount of data. Because these experiments have been applied to only a few organisms, and their accuracy is believed to be limited, it would be valuable to develop computational methods for predicting protein-protein interactions from their amino acid sequences or tertiary structural information.

Double-stranded DNA binding, an unusual property of DNA polymerase epsilon, promotes epigenetic silencing in Saccharomyces cerevisiae.

We have previously shown that DNA polymerase epsilon (Pol epsilon)of Saccharomyces cerevisiae binds stably to double-stranded DNA (dsDNA), a property not generally associated with DNA polymerases. Here, by reconstituting Pol epsilon activity from Pol2p-Dpb2p and Dpb3p-Dpb4p, its two component subassemblies, we report that Dpb3p-Dpb4p, a heterodimer of histone-fold motif-containing subunits, is responsible for the dsDNA binding. Substitution of specific lysine residues in Dpb3p, highlighted by homology modeling of Dpb3p-Dpb4p based on the structure of the histone H2A-H2B dimer, indicated that they play roles in binding of dsDNA by Dpb3p-Dpb4p, in a manner similar to the histone-DNA interaction.