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TitleThe Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region.
Journal, issue, pagesJ Struct Biol, Vol. 195, Issue 3, Page 316-324, Year 2016
Publish dateJul 12, 2016
AuthorsShintaro Aibara / Xiao-Chen Bai / Murray Stewart /
PubMed AbstractTranscription-export complex 2 (TREX-2 complex) facilitates the localization of actively transcribing genes to the nuclear periphery and also functions to contribute to the generation of export- ...Transcription-export complex 2 (TREX-2 complex) facilitates the localization of actively transcribing genes to the nuclear periphery and also functions to contribute to the generation of export-competent mRNPs through interactions with the general mRNA nuclear export factor Mex67:Mtr2. The TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31, and Sus1 bind. TREX-2 can be subdivided into two modules: one, in which Thp1 and Sem1 bind to the Sac3(M) region (residues ∼100-551), and the other in which Cdc31 and two Sus1 chains bind to the Sac3(CID) region (residues ∼710-805). Complementary structural analyses using X-ray crystallography, electron microscopy, and small-angle X-ray scattering of the Saccharomyces cerevisiae TREX-2 complex, expressed using Baculovirus-infected Sf9 cells, have indicated that the TPR-like repeats of the Sac3(M) region extend considerably further towards the N-terminus than previously thought, and also indicate that this region and Sac3(CID):Sus1:Cdc31 region of the S. cerevisiae complex are structurally independent. Although the density visible accounted for only ∼100kDa, a 5.3Å resolution cryo-EM reconstruction was obtained of the M-region of TREX-2 that showed an additional three putative α-helices extending towards the Sac3 N-terminus and these helices were also seen in a 4.9Å resolution structure obtained by X-ray crystallography.
SUMMARY STATEMENT: We describe the expression, purification and structural characterization of the S. cerevisiae TREX-2 complex and demonstrate that the Sac3 TPR-like repeats are more extensive than previously thought and that the M- and CID-regions do not appear to have a defined spatial orientation.
External linksJ Struct Biol / PubMed:27422657 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution4.927 - 5.3 Å
Structure data

3440

5g5p

EMDB-3440, PDB-5g5p:
Structure of the Saccharomyces cerevisiae TREX-2 complex
Method: EM (single particle) / Resolution: 5.3 Å

PDB-5l3t:
Structure of the Saccharomyces cerevisiae TREX-2 complex
Method: X-RAY DIFFRACTION / Resolution: 4.927 Å

Source
  • Saccharomyces cerevisae
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSPORT PROTEIN / MRNA / MRNA EXPORT / nuclear export / TREX-2 complex / Sac3 / Thp1

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