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KMID : 0578319960060060645
Molecules and Cells
1996 Volume.6 No. 6 p.645 ~ p.652
Identification of Human Liver cDNA Clones Whose Product Interact with G-Protein ¥â Subunit of Schizosccharomyces pombe
Won, Misun
Moon, Kyung-Mi/Jang, Young-Joo/Sun, Nam-Kyu/Kim, Dong-Uk/Han, Mi-Young/Lee, Chung-Eun
Abstract
Heterotrimeric GTP binding proteins (G-proteins) are composed of ¥á,¥â, and ¥ã subunits and have important roles in the cell signalling from cell surface receptors to effectors. The ¥á subunit as well as the ¥â¥ã complex are known to interact with effector molecules to deliver specific signals to downstream genes. In an attempt to identify the molecules interacting directly with G-protein ¥â subunit (G¥â) in signal pathway, G-protein ¥â subunit gene of Schizosaccharomyces pombe was used as bait to screen a human liver cDNA library in a yeast two-hybrid system. When the coding region DNA of the S.pombe ¥â subunit gene, gpb1^(+), was cloned into the 3¢¥-end of the GAL4 DNA binding domain sequence and used to screen a human liver cDNA library cloned at the 3¢¥-end of the GAL4 activation domain, 42 novel clones showing ¥â-galactosidase activiity were obtained from the 9¡¿10^(6) transformants. The sequence analysis of these clones revealed that the four clones contain sequence homologies with a receptor tyrosine kinase, a mammalian homolog of hsp40(DNAJ), a NMDA receptor glutamate-binding protein, and a protein serine kinase. These four clones showed specific binding to G-protein ¥â subunit of S.pombe in vitro. The characterization of these proteins in the G-protein-mediated signal pathway will be useful in elucidating the precise mechanism of G-protein function.
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