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Structure and Function of the TREX-2 Complex

  • Murray StewartEmail author
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 93)

Abstract

The Three prime repair exonuclease 2 (TREX-2) complex functions as a platform to which many of the components of the nuclear mRNA processing machinery bind, facilitating integration of this phase of the gene expression pathway, as well as mediating the re-positioning of highly regulated actively transcribing genes (such as GAL1) to nuclear pores (NPCs) to accelerate their activation. In Saccharomyces cerevisiae the TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31 and two Sus1 chains are bound. A combination of X-ray crystallography and electron microscopy studies have established the structure of two major regions of this complex: the M-region that functions to bind nucleic acids and the CID region that functions to link the complex to nuclear pores. These structures have facilitated the engineering of mutants that have been used to define the contributions made by the TREX-2 complex to locating high-expressed genes to nuclear pores and the contributions made to mRNA nuclear export.

Keywords

TREX-2 complex mRNA processing Nuclear pore NPC Karyopherin Chaperonin Nucleoporin 

Notes

Acknowledgements

Supported in part by MRC grants MC_U105178939, MC-A025-5PL41, MC_UP_1201/6 and a Leverhulme Emeritus Fellowship (EM-2016-062) to MS.

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.MRC Laboratory of Molecular BiologyCambridgeUK

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