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. 2001 Mar 9;276(10):7246-57.
doi: 10.1074/jbc.M004389200. Epub 2000 Nov 9.

Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B

T Sekiguchi  1 , E Hirose, N Nakashima, M Ii, T Nishimoto
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Free article

Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B

T Sekiguchi et al. J Biol Chem. .
Free article

Abstract

Rag A/Gtr1p are G proteins and are known to be involved in the RCC1-Ran pathway. We employed the two-hybrid method using Rag A as the bait to identify proteins binding to Rag A, and we isolated two novel human G proteins, Rag C and Rag D. Rag C demonstrates homology with Rag D (81.1% identity) and with Gtr2p of Saccharomyces cerevisiae (46.1% identity), and it belongs to the Rag A subfamily of the Ras family. Rag C and Rag D contain conserved GTP-binding motifs (PM-1, -2, and -3) in their N-terminal regions. Recombinant glutathione S-transferase fusion protein of Rag C efficiently bound to both [(3)H]GTP and [(3)H]GDP. Rag A was associated with both Rag C and Rag D in their C-terminal regions where a potential leucine zipper motif and a coiled-coil structure were found. Rag C and D were associated with both the GDP and GTP forms of Rag A. Both Rag C and Rag D changed their subcellular localization, depending on the nucleotide-bound state of Rag A. In a similar way, the disruption of S. cerevisiae GTR1 resulted in a change in the localization of Gtr2p.

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