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doi:10.1534/genetics.105.042366
A more recent version of this article appeared on August 1, 2005.
REGULAR RESEARCH PAPERS |
Association of GTP binding protein Gtr1p with Rpc19p, a shared subunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae
Yuko Todaka 1, Yonggang Wang 1, Kosuke Tashiro 1, Nobutaka Nakashima 1, Takeharu Nishimoto 1 and Takeshi Sekiguchi 1*
1 Kyushu University
* To whom correspondence should be addressed. E-mail: sekigu{at}molbiol.med.kyushu-u.ac.jp.
Submitted on February 22, 2005
Revised on April 6, 2005
Accepted on 11 April 2005
Yeast Gtr1p and its human homologue RRAG A belong to the Ras-like small G-protein superfamily and genetically interact with RCC1, a guanine nucleotide exchange factor for Ran GTPase. Little is known regarding the function of Gtr1p. We performed yeast two-hybrid screening using Gtr1p as the bait to find interacting proteins. Rpc19p, a shared subunit of RNA polymerases I and III, associated with Gtr1p. The association of Gtr1p with Rpc19p occurred in a GTP form - specific manner. RRAG A associated with RPA16 (human Rpc19p homologue) in a GTP form - specific manner, suggesting that the association is conserved during evolution. Ribosomal RNA and tRNA synthesis were reduced in the gtr1D strain expressing the GDP - form of Gtr1p, but not the GTP - form of Gtr1p. Gel filtration studies revealed an accumulation of the smaller Rpc19p-containing complex, but not of A135, in the gtr1D strain. Here, we propose that Gtr1p is involved in RNA polymerase I and III assembly by its association with Rpc19p and could be a mediator that links growth regulatory signals with ribosome biogenesis.
Key Words: GTR1, Ran, Rpc19p, ribosome RNA, transcription
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