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Title 

Mapping protein-protein proximity in the purinosome

Authors 

Y DengJongsik GamJ B FrenchH ZhaoS AnS J Benkovic

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2012

Citation 

Journal of Biological Chemistry, vol. 287, no. 43, pp. 36201-36207

Abstract 

The enzymes in the human de novo purine synthesis pathway were found to form a cellular complex, the purinosome, upon culturing cells in purine-depleted medium (An, S., Kumar R., Sheets, E. D., and Benkovic, S. J. (2008) Science 320, 103-106). Purinosome formation and dissociation were found to be modulated by several factors, including the microtubule network and cell signaling involving protein phosphorylation. To determine whether the pathway enzymes are in physical contact, we probed for the protein-protein interactions (PPIs) within the purinosome with a novel application of the Tango PPI reporter system (Barnea, G., Strapps, W., Herrada, G., Berman, Y., Ong, J., Kloss, B., Axel, R., and Lee, K. J. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 64-69). We found PPIs among all six enzymes within the pathway and evidence for a core involving the first three enzymes. We also captured purinosomes under both purine-rich and purine-depleted conditions. The results provide additional insights into the transient nature and topography of the purinosome.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M112.407056

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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