Protein-protein interactions of the hyperthermophilic archaeon Pyrococcus horikoshiiOT3 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2005-12

AUTHORS

Kengo Usui, Shintaro Katayama, Mutsumi Kanamori-Katayama, Chihiro Ogawa, Chikatoshi Kai, Makiko Okada, Jun Kawai, Takahiro Arakawa, Piero Carninci, Masayoshi Itoh, Koji Takio, Masashi Miyano, Satoru Kidoaki, Takehisa Matsuda, Yoshihide Hayashizaki, Harukazu Suzuki

ABSTRACT

BACKGROUND: Although 2,061 proteins of Pyrococcus horikoshii OT3, a hyperthermophilic archaeon, have been predicted from the recently completed genome sequence, the majority of proteins show no similarity to those from other organisms and are thus hypothetical proteins of unknown function. Because most proteins operate as parts of complexes to regulate biological processes, we systematically analyzed protein-protein interactions in Pyrococcus using the mammalian two-hybrid system to determine the function of the hypothetical proteins. RESULTS: We examined 960 soluble proteins from Pyrococcus and selected 107 interactions based on luciferase reporter activity, which was then evaluated using a computational approach to assess the reliability of the interactions. We also analyzed the expression of the assay samples by western blot, and a few interactions by in vitro pull-down assays. We identified 11 hetero-interactions that we considered to be located at the same operon, as observed in Helicobacter pylori. We annotated and classified proteins in the selected interactions according to their orthologous proteins. Many enzyme proteins showed self-interactions, similar to those seen in other organisms. CONCLUSION: We found 13 unannotated proteins that interacted with annotated proteins; this information is useful for predicting the functions of the hypothetical Pyrococcus proteins from the annotations of their interacting partners. Among the heterogeneous interactions, proteins were more likely to interact with proteins within the same ortholog class than with proteins of different classes. The analysis described here can provide global insights into the biological features of the protein-protein interactions in P. horikoshii. More... »

PAGES

r98

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/gb-2005-6-12-r98

DOI

http://dx.doi.org/10.1186/gb-2005-6-12-r98

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028915169

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16356270


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