Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development.

作者: Andrew G. DeMarco , Kedric L. Milholland , Amanda L. Pendleton , John J. Whitney , Peipei Zhu

DOI: 10.1038/S41598-020-68921-3

关键词:

摘要: Cdc14 protein phosphatases play an important role in plant infection by several fungal pathogens. This and other properties of enzymes make them intriguing target for development new antifungal crop treatments. Active site architecture substrate specificity from the model fungus Saccharomyces cerevisiae (ScCdc14) are well-defined unique among characterized phosphatases. appears absent some plants. However, extent conservation sequence, structure, pathogens is unknown. We addressed this performing a comprehensive phylogenetic analysis family comparing active structure sampling pathogen homologs. show that was lost common ancestor angiosperm plants but ubiquitous ascomycete basidiomycete fungi. The ScCdc14 invariant homologs eight diverse species dikarya, suggesting it conserved across lineage. A synthetic mimetic inhibited with similar low µM Ki values, had little effect on related Our results justify future exploration as broad spectrum protection.

参考文章(61)
Andrew J. Wiemer, David F. Wiemer, Prodrugs of Phosphonates and Phosphates: Crossing the Membrane Barrier Topics in Current Chemistry. ,vol. 360, pp. 115- 160 ,(2014) , 10.1007/128_2014_561
Z. Sheng, H. Charbonneau, The baculovirus Autographa californica encodes a protein tyrosine phosphatase. Journal of Biological Chemistry. ,vol. 268, pp. 4728- 4733 ,(1993) , 10.1016/S0021-9258(18)53457-8
Chaohui Li, Michael Melesse, Shijie Zhang, ChaoFeng Hao, Chenfang Wang, Hongchang Zhang, Mark C. Hall, Jin-Rong Xu, FgCDC14 regulates cytokinesis, morphogenesis, and pathogenesis in Fusarium graminearum Molecular Microbiology. ,vol. 98, pp. 770- 786 ,(2015) , 10.1111/MMI.13157
Eli Berdougo, Maxence V. Nachury, Peter K. Jackson, Prasad V. Jallepalli, The nucleolar phosphataseCdc14Bis dispensable for chromosome segregation and mitotic exit in human cells Cell Cycle. ,vol. 7, pp. 1184- 1190 ,(2008) , 10.4161/CC.7.9.5792
Steven C. Bremmer, Hana Hall, Juan S. Martinez, Christie L. Eissler, Thomas H. Hinrichsen, Sandra Rossie, Laurie L. Parker, Mark C. Hall, Harry Charbonneau, Cdc14 Phosphatases Preferentially Dephosphorylate a Subset of Cyclin-dependent kinase (Cdk) Sites Containing Phosphoserine Journal of Biological Chemistry. ,vol. 287, pp. 1662- 1669 ,(2012) , 10.1074/JBC.M111.281105
Fabio Cerignoli, Souad Rahmouni, Ze’ev Ronai, Tomas Mustelin, Regulation of MAP kinases by the VHR dual-specific phosphatase: implications for cell growth and differentiation. Cell Cycle. ,vol. 5, pp. 2210- 2215 ,(2006) , 10.4161/CC.5.19.3267
Christie L. Eissler, Gerard Mazón, Brendan L. Powers, Sergey N. Savinov, Lorraine S. Symington, Mark C. Hall, The Cdk/Cdc14 Module Controls Activation of the Yen1 Holliday Junction Resolvase to Promote Genome Stability Molecular Cell. ,vol. 54, pp. 80- 93 ,(2014) , 10.1016/J.MOLCEL.2014.02.012
Kaushik Panigrahi, MariJean Eggen, Jun-Ho Maeng, Quanrong Shen, David B. Berkowitz, The α,α-Difluorinated Phosphonate L-pSer-Analogue: An Accessible Chemical Tool for Studying Kinase- Dependent Signal Transduction Chemistry & Biology. ,vol. 16, pp. 928- 936 ,(2009) , 10.1016/J.CHEMBIOL.2009.08.008