A protein linkage map of Escherichia coli bacteriophage T7.
Genome sequencing projects are predicting large numbers of novel proteins, whose interactions with other proteins must mediate the function of cellular processes. To analyse these networks, we used the yeast two-hybrid system on a genome-wide scale to identify 25 interactions among the proteins of Escherichia coli bacteriophage T7. Among these is a set of six interactions connecting proteins that function in DNA replication and DNA packaging. Remarkably, two genes, arranged such that one entirely overlaps the other and uses a different reading frame, encode interacting proteins. Several of the interactions reflect intramolecular associations of different domains of the same polypeptide, suggesting that the two-hybrid assay may be useful in the analysis of protein folding. This global approach to protein-protein interactions may be applicable to the analysis of more complex genomes whose sequences are becoming available.
Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook 11794, USA.
P L
PL
Bartel
J A
JA
Roecklein
D
D
SenGupta
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S
Fields
D000595:Amino Acid Sequence; D017123:Bacteriophage T7 / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure*; D001483:Base Sequence; D017931:DNA Primers / Q000737:chemistry; D004261:DNA Replication; D005807:Genes, Overlapping; D005822:Genetic Vectors; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
D017931:DNA Primers; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D014764:Viral Proteins