The protein-protein interaction map of Helicobacter pylori.
With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function. As elementary constituents of cellular protein complexes and pathways, protein-protein interactions are key determinants of protein function. Here we have built a large-scale protein-protein interaction map of the human gastric pathogen Helicobacter pylori. We have used a high-throughput strategy of the yeast two-hybrid assay to screen 261 H. pylori proteins against a highly complex library of genome-encoded polypeptides. Over 1,200 interactions were identified between H. pylori proteins, connecting 46.6% of the proteome. The determination of a reliability score for every single protein-protein interaction and the identification of the actual interacting domains permitted the assignment of unannotated proteins to biological pathways.
Rain
J C
JC
Hybrigenics SA, Paris, France.
Selig
L
L
De Reuse
H
H
Battaglia
V
V
Reverdy
C
C
Simon
S
S
Lenzen
G
G
Petel
F
F
Wojcik
J
J
Schächter
V
V
Chemama
Y
Y
Labigne
A
A
Legrain
P
P
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D016208:Databases, Factual; D004926:Escherichia coli / Q000235:genetics; D015723:Gene Library; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D020407:Internet; D008969:Molecular Sequence Data; D011485:Protein Binding; D020543:Proteome; D016415:Sequence Alignment; D012984:Software; D014510:Urease / Q000378:metabolism
D001426:Bacterial Proteins; D020543:Proteome; D014510:Urease