PT  - JOURNAL ARTICLE
AU  - Lianhu Zhang
AU  - Dongmei Zhang
AU  - Yunyun Chen
AU  - Wenyu Ye
AU  - Quinyun Lin
AU  - Goudong Lu
AU  - Daniel J. Ebbole
AU  - Stefan Olsson
AU  - Zonghua Wang
TI  - Localization and protein-protein interactions of protein kinase CK2 suggest a chaperone-like activity is integral to its function in <em>M. oryzae</em>
AID  - 10.1101/323816
DP  - 2018 Jan 01
TA  - bioRxiv
PG  - 323816
4099  - http://biorxiv.org/content/early/2018/05/16/323816.short
4100  - http://biorxiv.org/content/early/2018/05/16/323816.full
AB  - CK2 is a constitutively active conserved serine/threonine kinase in eukaryotes. We characterized three components of the CK2 holoenzyme, CKa, CKb1 and CKb2, in the fungus Magnaporthe oryzae. The CKa encoding gene appears to be essential. All three CK2 components were localized with GFP fusions and both CKb components were needed for preferential cellular localization to the nucleolus and as structures at septal pores. A unique CK2 filament was prominent within appressoria. A pulldown experiment identified CKa interacting proteins with an overrepresentation of intrinsically unfolded proteins containing a CK2 phosphorylation motif for destabilizing and unfolding alpha helixes. This suggests a role for CK2 in forming protein aggregates. Supporting this conclusion, we found that CKa expression and a key autophagy gene, Atg8, are strongly correlated, indicating that an increased removal of aggregates is needed with higher CKa expression.