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|Title:||A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa||Authors:||Yuan, P.
|Issue Date:||1-Apr-2003||Citation:||Yuan, P., Jedd, G., Kumaran, D., Swaminathan, S., Shio, H., Hewitt, D., Chua, N.-H., Swaminathan, K. (2003-04-01). A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa. Nature Structural Biology 10 (4) : 264-270. ScholarBank@NUS Repository. https://doi.org/10.1038/nsb910||Abstract:||The Woronin body is a dense-core vesicle specific to filamentous ascomycetes (Euascomycetes), where it functions to seal the septal pore in response to cellular damage. The HEX-1 protein self-assembles to form this solid core of the vesicle. Here, we solve the crystal structure of HEX-1 at 1.8 Å, which provides the structural basis of its selfassembly. The structure reveals the existence of three intermolecular interfaces that promote the formation of a three-dimensional protein lattice. Consistent with these data, self-assembly is disrupted by mutations in intermolecular contact residues and expression of an assembly-defective HEX-1 mutant results in the production of aberrant Woronin bodies, which possess a soluble noncrystalline core. This mutant also fails to complement a hex-1 deletion in Neurospora crassa, demonstrating that the HEX-1 protein lattice is required for Woronin body function. Although both the sequence and the tertiary structure of HEX-1 are similar to those of eukaryotic initiation factor 5A (elF-5A), the amino acids required for HEX-1 self-assembly and peroxisomal targeting are absent in elF-5A. Thus, we propose that a new function has evolved following duplication of an ancestral elF-5A gene and that this may define an important step in fungal evolution.||Source Title:||Nature Structural Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/99840||ISSN:||10728368||DOI:||10.1038/nsb910|
|Appears in Collections:||Staff Publications|
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