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PMID: 19674973 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.

The Journal of biological chemistry ·Vol. 284 ·No. 41 ·2009-10-09 ·Pages 28442-28452

Whittle JRR, Schwartz TU

Abstract

The nuclear pore complex (NPC) constitutes one of the largest protein assemblies in the eukaryotic cell and forms the exclusive gateway to the nucleus. The stable, approximately 15-20-MDa scaffold ring of the NPC is built from two multiprotein complexes arranged around a central 8-fold axis. Here we present crystal structures of two large architectural units, yNup170(979-1502) and hNup107(658-925) x hNup133(517-1156), each a constituent of one of the two multiprotein complexes. Conservation of domain arrangement and of tertiary structure suggests that Nup157/170 and Nup133 derived from a common ancestor. Together with the previously established ancestral coatomer element (ACE1), these two elements constitute the major alpha-helical building blocks of the NPC scaffold and define its branched, lattice-like architecture, similar to vesicle coats like COPII. We hypothesize that the extant NPC evolved early during eukaryotic evolution from a rudimentary structure composed of several identical copies of a few ancestral elements, later diversified and specified by gene duplication.

MeSH Terms
Amino Acid Sequence Crystallography, X-Ray Evolution, Molecular Humans Minor Histocompatibility Antigens Models, Molecular Molecular Sequence Data Multiprotein Complexes/chemistry,metabolism Nuclear Pore/chemistry,metabolism Nuclear Pore Complex Proteins/chemistry,genetics,metabolism Protein Structure, Secondary Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Minor Histocompatibility Antigens Multiprotein Complexes NUP107 protein, human NUP133 protein, human NUP157 protein, S cerevisiae NUP170 protein, S cerevisiae NUP84 protein, S cerevisiae Nuclear Pore Complex Proteins Saccharomyces cerevisiae Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Whittle James R R
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Schwartz Thomas U
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139. Electronic address: tus@mit.edu.
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Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
1083-351X
Published
2009-10-09
Epub
2009-00-11
Pages
28442-28452
Language
English
Region
United States
NLM ID
2985121R
PMCID
PMC2788893
Subset
IM
Grants
NIGMS NIH HHS · R01 GM077537 · United States
NIGMS NIH HHS · GM77537 · United States
Databases
PDB
Analysis Services
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