High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1

Julian O. B. Jacobsen, Mark D. Allen, Stefan M. V. Freund, Mark Bycroft

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THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. THO is thought to be formed from five subunits, Tho2p, Hpr1p, Tex1p, Mft1p and Thp2p, and recent work has determined a low-resolution structure of the complex [Poulsen et al. (2014), PLoS One, 9, e103470]. A number of additional proteins are thought to be involved in the formation of mRNP in yeast, including Tho1, which has been shown to bind RNA in vitro and is recruited to actively transcribed chromatin in vivo in a THO-complex and RNA-dependent manner. Tho1 is known to contain a SAP domain at the N-terminus, but the ability to suppress the expression defects of the hpr1Δ mutant of THO was shown to reside in the RNA-binding C-terminal region. In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and C-terminal RNA-binding domain have been determined.
Original languageEnglish
Pages (from-to)500-506
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number6
Early online date23 May 2016
Publication statusPublished - 1 Jun 2016
Externally publishedYes


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