期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1997
卷号：94
期号：16
页码：8405-8410
DOI：10.1073/pnas.94.16.8405
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：We present an approach for monitoring protein-protein interactions within intact eukaryotic cells, which should increase our understanding of the regulatory circuitry that controls the proliferation and differentiation of cells and how these processes go awry in disease states such as cancer. Chimeric proteins composed of proteins of interest fused to complementing {beta}-galactosidase ({beta}-gal) deletion mutants permit a novel analysis of protein complexes within cells. In this approach, the {beta}-gal activity resulting from the forced interaction of nonfunctional weakly complementing {beta}-gal peptides ({Delta} and {Delta}{omega}) serves as a measure of the extent of interaction of the non-{beta}-gal portions of the chimeras. To test this application of lacZ intracistronic complementation, proteins that form a complex in the presence of rapamycin were used. These proteins, FRAP and FKBP12, were synthesized as fusion proteins with {Delta} and {Delta}{omega
