Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Parthasarathy Sampathkumar; Seung Joong Kim; Danalyn Manglicmot; Kevin T. Bain; Jeremiah Gilmore; Tarun Gheyi; Jeremy Phillips; Ursula Pieper; Javier Fernandez-Martinez; Josef D. Franke; Tsutomu Matsui; Hiro Tsuruta; Shane Atwell; Devon A. Thompson; J. Spencer Emtage; Stephen R. Wasserman; Michael P. Rout; Andrej Sali; J. Michael Sauder; Steven C. Almo; Stephen K. Burley

doi:10.1002/prot.24102

Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Parthasarathy Sampathkumar, Seung Joong Kim, Danalyn Manglicmot, Kevin T. Bain, Jeremiah Gilmore, Tarun Gheyi, Jeremy Phillips, Ursula Pieper, Javier Fernandez-Martinez, Josef D. Franke, Tsutomu Matsui, Hiro Tsuruta, Shane Atwell, Devon A. Thompson, J. Spencer Emtage, Stephen R. Wasserman, Michael P. Rout, Andrej Sali, J. Michael Sauder, Steven C. AlmoStephen K. Burley

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal "FG" repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 882-1034 [CgNup116(882-1034)], at 1.94 Å resolution. The X-ray structure of CgNup116(882-1034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(882-1034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed.

Original language	English (US)
Pages (from-to)	2110-2116
Number of pages	7
Journal	Proteins: Structure, Function and Bioinformatics
Volume	80
Issue number	8
DOIs	https://doi.org/10.1002/prot.24102
State	Published - Aug 2012

Keywords

MRNA export
Nuclear pore complex
Nup100
Nup116
Nup145
Nup98
Structural genomics

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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Sampathkumar, P., Kim, S. J., Manglicmot, D., Bain, K. T., Gilmore, J., Gheyi, T., Phillips, J., Pieper, U., Fernandez-Martinez, J., Franke, J. D., Matsui, T., Tsuruta, H., Atwell, S., Thompson, D. A., Emtage, J. S., Wasserman, S. R., Rout, M. P., Sali, A., Sauder, J. M., ... Burley, S. K. (2012). Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata. Proteins: Structure, Function and Bioinformatics, 80(8), 2110-2116. https://doi.org/10.1002/prot.24102

Sampathkumar, P, Kim, SJ, Manglicmot, D, Bain, KT, Gilmore, J, Gheyi, T, Phillips, J, Pieper, U, Fernandez-Martinez, J, Franke, JD, Matsui, T, Tsuruta, H, Atwell, S, Thompson, DA, Emtage, JS, Wasserman, SR, Rout, MP, Sali, A, Sauder, JM, Almo, SC & Burley, SK 2012, 'Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata', Proteins: Structure, Function and Bioinformatics, vol. 80, no. 8, pp. 2110-2116. https://doi.org/10.1002/prot.24102

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title = "Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata",

abstract = "The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal {"}FG{"} repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 882-1034 [CgNup116(882-1034)], at 1.94 {\AA} resolution. The X-ray structure of CgNup116(882-1034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(882-1034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed.",

keywords = "MRNA export, Nuclear pore complex, Nup100, Nup116, Nup145, Nup98, Structural genomics",

author = "Parthasarathy Sampathkumar and Kim, {Seung Joong} and Danalyn Manglicmot and Bain, {Kevin T.} and Jeremiah Gilmore and Tarun Gheyi and Jeremy Phillips and Ursula Pieper and Javier Fernandez-Martinez and Franke, {Josef D.} and Tsutomu Matsui and Hiro Tsuruta and Shane Atwell and Thompson, {Devon A.} and Emtage, {J. Spencer} and Wasserman, {Stephen R.} and Rout, {Michael P.} and Andrej Sali and Sauder, {J. Michael} and Almo, {Steven C.} and Burley, {Stephen K.}",

year = "2012",

month = aug,

doi = "10.1002/prot.24102",

language = "English (US)",

volume = "80",

pages = "2110--2116",

journal = "Proteins: Structure, Function and Bioinformatics",

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publisher = "Wiley-Liss Inc.",

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T1 - Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

AU - Sampathkumar, Parthasarathy

AU - Kim, Seung Joong

AU - Manglicmot, Danalyn

AU - Bain, Kevin T.

AU - Gilmore, Jeremiah

AU - Gheyi, Tarun

AU - Phillips, Jeremy

AU - Pieper, Ursula

AU - Fernandez-Martinez, Javier

AU - Franke, Josef D.

AU - Matsui, Tsutomu

AU - Tsuruta, Hiro

AU - Atwell, Shane

AU - Thompson, Devon A.

AU - Emtage, J. Spencer

AU - Wasserman, Stephen R.

AU - Rout, Michael P.

AU - Sali, Andrej

AU - Sauder, J. Michael

AU - Almo, Steven C.

AU - Burley, Stephen K.

PY - 2012/8

Y1 - 2012/8

N2 - The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal "FG" repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 882-1034 [CgNup116(882-1034)], at 1.94 Å resolution. The X-ray structure of CgNup116(882-1034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(882-1034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed.

AB - The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal "FG" repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 882-1034 [CgNup116(882-1034)], at 1.94 Å resolution. The X-ray structure of CgNup116(882-1034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(882-1034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed.

KW - MRNA export

KW - Nuclear pore complex

KW - Nup100

KW - Nup116

KW - Nup145

KW - Nup98

KW - Structural genomics

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U2 - 10.1002/prot.24102

DO - 10.1002/prot.24102

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C2 - 22544723

AN - SCOPUS:84863782663

SN - 0887-3585

VL - 80

SP - 2110

EP - 2116

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

IS - 8

ER -

Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Abstract

Keywords

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