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Sem1

A versatile "molecular glue"?

Pages 12-17 | Received 14 Sep 2009, Accepted 23 Oct 2009, Published online: 01 Jan 2010

Figures & data

Figure 1 mRNA export and gene gating in S. cerevisiae. (A) The THO complex is co-transcriptionally recruited and associates with nascent transcripts. Together with Sub2 and Yra1 the trEx complex is formed. Mex67-Mtr2 binds to the mrNPs through adaptor proteins such as Yra1 and facilitates their nuclear export. (B) Interactions between the SAGA transcription initiation complex and the nuclear pore associated TREX-2 complex result in tethering of activated genes to the nuclear periphery.

Figure 1 mRNA export and gene gating in S. cerevisiae. (A) The THO complex is co-transcriptionally recruited and associates with nascent transcripts. Together with Sub2 and Yra1 the trEx complex is formed. Mex67-Mtr2 binds to the mrNPs through adaptor proteins such as Yra1 and facilitates their nuclear export. (B) Interactions between the SAGA transcription initiation complex and the nuclear pore associated TREX-2 complex result in tethering of activated genes to the nuclear periphery.

Figure 2 Association of Sem1 with target complexes. The RP of the proteasome, TREX-2 and the CSN are the three complexes in budding yeast, which contain PAM and Sac3_GANP domains and feature Sem1 as a component.

Figure 2 Association of Sem1 with target complexes. The RP of the proteasome, TREX-2 and the CSN are the three complexes in budding yeast, which contain PAM and Sac3_GANP domains and feature Sem1 as a component.

Figure 3 Models for interaction of Sem1 with Sac3_GANP and PAM domains. Depending on the ability of Sem1 to interact with PAM and Sac3_GANP domains individually, we propose two distinct models: in (a) Sem1 is not able to interact with PAM or Sac3_GANP domains individually and therefore association of Sem1 necessitates an interaction of these domains prior to binding. In model (B), Sem1 can interact with PAM and Sac3_GANP domains individually and thereby bridge these domains.

Figure 3 Models for interaction of Sem1 with Sac3_GANP and PAM domains. Depending on the ability of Sem1 to interact with PAM and Sac3_GANP domains individually, we propose two distinct models: in (a) Sem1 is not able to interact with PAM or Sac3_GANP domains individually and therefore association of Sem1 necessitates an interaction of these domains prior to binding. In model (B), Sem1 can interact with PAM and Sac3_GANP domains individually and thereby bridge these domains.