Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex.
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nup133 beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex.
Berke
Ian C
IC
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA.
Boehmer
Thomas
T
Blobel
Günter
G
Schwartz
Thomas U
TU
D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000595:Amino Acid Sequence / Q000502:physiology; D017124:Conserved Sequence / Q000502:physiology; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D006367:HeLa Cells; D006801:Humans; D015778:Minor Histocompatibility Antigens; D008958:Models, Molecular; D022022:Nuclear Pore / Q000737:chemistry*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000502:physiology; D017386:Sequence Homology, Amino Acid
D015778:Minor Histocompatibility Antigens; C440250:NUP133 protein, human; D028861:Nuclear Pore Complex Proteins