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==Crystal structure of Saccharomyces cerevisiae Gle1 CTD-Nup42 GBM complex==
==Crystal structure of Saccharomyces cerevisiae Gle1 CTD-Nup42 GBM complex==
<StructureSection load='6b4e' size='340' side='right' caption='[[6b4e]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='6b4e' size='340' side='right'caption='[[6b4e]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6b4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B4E FirstGlance]. <br>
<table><tr><td colspan='2'>[[6b4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B4E FirstGlance]. <br>
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==See Also==
==See Also==
*[[Nucleoporin|Nucleoporin]]
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Baker's yeast]]
[[Category: Baker's yeast]]
[[Category: Large Structures]]
[[Category: Cai, S W]]
[[Category: Cai, S W]]
[[Category: Correia, A R]]
[[Category: Correia, A R]]

Revision as of 20:09, 20 November 2019

Crystal structure of Saccharomyces cerevisiae Gle1 CTD-Nup42 GBM complexCrystal structure of Saccharomyces cerevisiae Gle1 CTD-Nup42 GBM complex

Structural highlights

6b4e is a 4 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:GLE1, BRR3, RSS1, YDL207W, D1049 (Baker's yeast), NUP42, RIP1, UIP1, YDR192C, YD9346.04C (Baker's yeast)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLE1_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonuleoprotein (hnRNP) NAB2 from exported mRNA.[1] [2] [3] [4] [5] [NUP42_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP42 is specifically important for nuclear protein and mRNA export.[6] [7] [8] [9] [10] [11] [12] [13]

Publication Abstract from PubMed

The nuclear pore complex (NPC) controls the passage of macromolecules between the nucleus and cytoplasm, but how the NPC directly participates in macromolecular transport remains poorly understood. In the final step of mRNA export, the DEAD-box helicase DDX19 is activated by the nucleoporins Gle1, Nup214, and Nup42 to remove Nxf1*Nxt1 from mRNAs. Here, we report crystal structures of Gle1*Nup42 from three organisms that reveal an evolutionarily conserved binding mode. Biochemical reconstitution of the DDX19 ATPase cycle establishes that human DDX19 activation does not require IP6, unlike its fungal homologs, and that Gle1 stability affects DDX19 activation. Mutations linked to motor neuron diseases cause decreased Gle1 thermostability, implicating nucleoporin misfolding as a disease determinant. Crystal structures of human Gle1*Nup42*DDX19 reveal the structural rearrangements in DDX19 from an auto-inhibited to an RNA-binding competent state. Together, our results provide the foundation for further mechanistic analyses of mRNA export in humans.

Structural and functional analysis of mRNA export regulation by the nuclear pore complex.,Lin DH, Correia AR, Cai SW, Huber FM, Jette CA, Hoelz A Nat Commun. 2018 Jun 13;9(1):2319. doi: 10.1038/s41467-018-04459-3. PMID:29899397[14]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Hodge CA, Colot HV, Stafford P, Cole CN. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 1999 Oct 15;18(20):5778-88. PMID:10523319 doi:10.1093/emboj/18.20.5778
  2. ↑ Strahm Y, Fahrenkrog B, Zenklusen D, Rychner E, Kantor J, Rosbach M, Stutz F. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 1999 Oct 15;18(20):5761-77. PMID:10610322 doi:10.1093/emboj/18.20.5761
  3. ↑ Rout MP, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, Chait BT. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol. 2000 Feb 21;148(4):635-51. PMID:10684247
  4. ↑ Jensen TH, Patricio K, McCarthy T, Rosbash M. A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription. Mol Cell. 2001 Apr;7(4):887-98. PMID:11336711
  5. ↑ Suntharalingam M, Alcazar-Roman AR, Wente SR. Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function. J Biol Chem. 2004 Aug 20;279(34):35384-91. Epub 2004 Jun 18. PMID:15208322 doi:10.1074/jbc.M402044200
  6. ↑ Hodge CA, Colot HV, Stafford P, Cole CN. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 1999 Oct 15;18(20):5778-88. PMID:10523319 doi:10.1093/emboj/18.20.5778
  7. ↑ Strahm Y, Fahrenkrog B, Zenklusen D, Rychner E, Kantor J, Rosbach M, Stutz F. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 1999 Oct 15;18(20):5761-77. PMID:10610322 doi:10.1093/emboj/18.20.5761
  8. ↑ Vainberg IE, Dower K, Rosbash M. Nuclear export of heat shock and non-heat-shock mRNA occurs via similar pathways. Mol Cell Biol. 2000 Jun;20(11):3996-4005. PMID:10805742
  9. ↑ Strasser K, Bassler J, Hurt E. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J Cell Biol. 2000 Aug 21;150(4):695-706. PMID:10952996
  10. ↑ Allen NP, Huang L, Burlingame A, Rexach M. Proteomic analysis of nucleoporin interacting proteins. J Biol Chem. 2001 Aug 3;276(31):29268-74. Epub 2001 May 31. PMID:11387327 doi:http://dx.doi.org/10.1074/jbc.M102629200
  11. ↑ Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2450-5. Epub 2003 Feb 25. PMID:12604785 doi:10.1073/pnas.0437902100
  12. ↑ Pyhtila B, Rexach M. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J Biol Chem. 2003 Oct 24;278(43):42699-709. Epub 2003 Aug 12. PMID:12917401 doi:http://dx.doi.org/10.1074/jbc.M307135200
  13. ↑ Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol. 2004 Mar;6(3):197-206. Epub 2004 Feb 22. PMID:15039779 doi:10.1038/ncb1097
  14. ↑ Lin DH, Correia AR, Cai SW, Huber FM, Jette CA, Hoelz A. Structural and functional analysis of mRNA export regulation by the nuclear pore complex. Nat Commun. 2018 Jun 13;9(1):2319. doi: 10.1038/s41467-018-04459-3. PMID:29899397 doi:http://dx.doi.org/10.1038/s41467-018-04459-3

6b4e, resolution 1.75Å

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