Journal: J Struct Biol / Year: 2016 Title: The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. Authors: Shintaro Aibara / Xiao-Chen Bai / Murray Stewart / Abstract: 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- ...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 ...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.
History
Deposition
May 26, 2016
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Header (metadata) release
Jul 27, 2016
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Map release
Jul 27, 2016
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Update
Nov 23, 2016
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Current status
Nov 23, 2016
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Supramolecule #1000: Sac3 in complex with Thp1 and Sem1
Supramolecule
Name: Sac3 in complex with Thp1 and Sem1 / type: sample / ID: 1000 / Details: Sample is monodisperse / Oligomeric state: One heterotrimer / Number unique components: 3
Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 85 K / Instrument: HOMEMADE PLUNGER / Method: Blot for 7 seconds before plunging from one side
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Electron microscopy
Microscope
FEI TITAN KRIOS
Temperature
Min: 80 K / Max: 90 K / Average: 85 K
Specialist optics
Energy filter - Name: Gatan Quantum / Energy filter - Lower energy threshold: 0.0 eV / Energy filter - Upper energy threshold: 20.0 eV
Date
Nov 3, 2015
Image recording
Category: CCD / Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 40 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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