Please use this identifier to cite or link to this item:
|Title:||A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa|
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Nov 9, 2018
WEB OF SCIENCETM
checked on Nov 12, 2018
checked on Oct 26, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.