8h5b: Difference between revisions

Latest revision as of 14:43, 20 September 2023

The cryo-EM structure of nuclear transport receptor Kap114p complex with yeast TATA-box binding protein

Structural highlights

8h5b is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4.03Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IMB5_YEAST Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA-binding protein (TBP) and of histones H2A and H2B.^[1] ^[2]

Publication Abstract from PubMed

The transcription factor TATA-box binding protein (TBP) modulates gene expression in nuclei. This process requires the involvement of nuclear transport receptors, collectively termed karyopherin-beta (Kap-beta) in yeast, and various regulatory factors. In previous studies we showed that Kap114p, a Kap-beta that mediates nuclear import of yeast TBP (yTBP), modulates yTBP-dependent transcription. However, how Kap114p associates with yTBP to exert its multifaceted functions has remained elusive. Here, we employ single-particle cryo-electron microscopy to determine the structure of Kap114p in complex with the core domain of yTBP (yTBP(C)). Remarkably, Kap114p wraps around the yTBP(C) N-terminal lobe, revealing a structure resembling transcriptional regulators in complex with TBP, suggesting convergent evolution of the two protein groups for a common function. We further demonstrate that Kap114p sequesters yTBP away from promoters, preventing a collapse of yTBP dynamics required for yeast responses to environmental stress. Hence, we demonstrate that nuclear transport receptors represent critical elements of the transcriptional regulatory network.

Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein.,Liao CC, Wang YS, Pi WC, Wang CH, Wu YM, Chen WY, Hsia KC Nat Commun. 2023 Sep 8;14(1):5518. doi: 10.1038/s41467-023-41206-9. PMID:37684250^[3]

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

References

↑ Morehouse H, Buratowski RM, Silver PA, Buratowski S. The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12542-7. PMID:10535958
↑ Mosammaparast N, Jackson KR, Guo Y, Brame CJ, Shabanowitz J, Hunt DF, Pemberton LF. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J Cell Biol. 2001 Apr 16;153(2):251-62. PMID:11309407
↑ Liao CC, Wang YS, Pi WC, Wang CH, Wu YM, Chen WY, Hsia KC. Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein. Nat Commun. 2023 Sep 8;14(1):5518. PMID:37684250 doi:10.1038/s41467-023-41206-9

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Morehouse H, Buratowski RM, Silver PA, Buratowski S. The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12542-7. PMID:10535958

[2] Mosammaparast N, Jackson KR, Guo Y, Brame CJ, Shabanowitz J, Hunt DF, Pemberton LF. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J Cell Biol. 2001 Apr 16;153(2):251-62. PMID:11309407

[3] Liao CC, Wang YS, Pi WC, Wang CH, Wu YM, Chen WY, Hsia KC. Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein. Nat Commun. 2023 Sep 8;14(1):5518. PMID:37684250 doi:10.1038/s41467-023-41206-9

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8h5b is ON HOLD  until Paper Publication
+==The cryo-EM structure of nuclear transport receptor Kap114p complex with yeast TATA-box binding protein==
+<StructureSection load='8h5b' size='340' side='right'caption='[[8h5b]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8h5b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H5B FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.03&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8h5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h5b OCA], [https://pdbe.org/8h5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h5b RCSB], [https://www.ebi.ac.uk/pdbsum/8h5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h5b ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IMB5_YEAST IMB5_YEAST] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA-binding protein (TBP) and of histones H2A and H2B.<ref>PMID:10535958</ref> <ref>PMID:11309407</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The transcription factor TATA-box binding protein (TBP) modulates gene expression in nuclei. This process requires the involvement of nuclear transport receptors, collectively termed karyopherin-beta (Kap-beta) in yeast, and various regulatory factors. In previous studies we showed that Kap114p, a Kap-beta that mediates nuclear import of yeast TBP (yTBP), modulates yTBP-dependent transcription. However, how Kap114p associates with yTBP to exert its multifaceted functions has remained elusive. Here, we employ single-particle cryo-electron microscopy to determine the structure of Kap114p in complex with the core domain of yTBP (yTBP(C)). Remarkably, Kap114p wraps around the yTBP(C) N-terminal lobe, revealing a structure resembling transcriptional regulators in complex with TBP, suggesting convergent evolution of the two protein groups for a common function. We further demonstrate that Kap114p sequesters yTBP away from promoters, preventing a collapse of yTBP dynamics required for yeast responses to environmental stress. Hence, we demonstrate that nuclear transport receptors represent critical elements of the transcriptional regulatory network.
-Authors: Hsia, K.C., Liao, C.C., Wang, C.H., Wu, Y.M.
+Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein.,Liao CC, Wang YS, Pi WC, Wang CH, Wu YM, Chen WY, Hsia KC Nat Commun. 2023 Sep 8;14(1):5518. doi: 10.1038/s41467-023-41206-9. PMID:37684250<ref>PMID:37684250</ref>
-Description: The cryo-EM structure of nuclear transport receptor Kap114p complex with yeast TATA-box binding protein
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Hsia, K.C]]
+<div class="pdbe-citations 8h5b" style="background-color:#fffaf0;"></div>
-[[Category: Wu, Y.M]]
+== References ==
-[[Category: Wang, C.H]]
+<references/>
-[[Category: Liao, C.C]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Hsia KC]]
+[[Category: Liao CC]]
+[[Category: Wang CH]]
+[[Category: Wu YM]]

8h5b: Difference between revisions

Latest revision as of 14:43, 20 September 2023

The cryo-EM structure of nuclear transport receptor Kap114p complex with yeast TATA-box binding protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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