| Description | This N-terminal domain, HeLo, has a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation [ ]. The domain is found exclusively in the fungal kingdom. Its structure, as it occurs in the heterokaryon incompatibility proteins HET-s and HET-S proteins, consists of two bundles of α-helices that pack into a single globular domain []. The domain boundary determined from its structure and from protease-resistance experiments overlaps with the C-terminal prion-forming domain of HET-s [ ]. The HeLo domains of HET-s and HET-S are very similar and their few differences (and not the prion-forming domains) determine the compatibility-phenotype of the fungi in which the proteins are expressed.The mechanism of the HeLo domain-function in heterokaryon-incompatibility is still under investigation, however the HeLo domain is found in similar protein architectures as other cell death and apoptosis-inducing domains. The only other HeLo protein to which a function has been associated is LopB from Leptosphaeria maculans [ ]. Although its specific role in L. maculans is unknown, LopB- mutants have impaired ability to form lesions on oilseed rape. The HeLo domain is not related to the HET domain () which is another domain involved in heterokaryon incompatibility. | Name | Prion-inhibition and propagation, HeLo domain |
| Short Name | HeLo_dom | Type | Domain |
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