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Protist

Title:		A novel protein kinase from the ciliate Euplotes raikovi with close structural identity to the mammalian intestinal and male-germ cell kinases: characterization and functional implications in the autocrine pheromone signaling loop
Author(s):		Vallesi A; Di Pretoro B; Ballarini P; Apone F; Luporini P;
Address:		"Dipartimento di Scienze Ambientali e Naturali, University of Camerino, via Gentile III da Varano, 62032 Camerino (MC), Italy. adriana.vallesi@unicam.it"
Journal Title:		Protist
Year:		2010
Volume:		20100113
Issue:		2
Page Number:		250 - 263
DOI:		10.1016/j.protis.2009.12.002
ISSN/ISBN:		1618-0941 (Electronic) 1434-4610 (Linking)
Abstract:		"In the free-living ciliate Euplotes raikovi, we identified (and designated as Er-MAPK1) a protein kinase of 631 amino acids, that appears to be constantly phosphorylated in cells which are in growth stage and interact in autocrine fashion with their water-soluble signal pheromones. Er-MAPK1 is specified by a gene that requires a+1 translational frame-shift to be expressed. Its amino-terminal region represents a canonical catalytic domain and carries an activation loop distinctive of the mitogen-activated protein kinases, with the Thr-Asp-Tyr motif deputed to be site of double phosphorylation. In contrast, the carboxy-terminal region appears to be structurally unique. It shows a strongly basic amino acid composition, is very rich in glycine repetitions, and contains a bipartite signal for translocation of Er-MAPK1 into the nucleus"
Keywords:		"Active Transport, Cell Nucleus Amino Acid Sequence Animals Base Sequence Catalytic Domain Euplotes/*enzymology/*physiology Frameshifting, Ribosomal Male Molecular Sequence Data Pheromones/*metabolism Phylogeny Protein Binding Protein Biosynthesis Protein;"
Notes:		"MedlineVallesi, Adriana Di Pretoro, Barbara Ballarini, Patrizia Apone, Fabio Luporini, Pierangelo eng Research Support, Non-U.S. Gov't Germany 2010/01/16 Protist. 2010 Apr; 161(2):250-63. doi: 10.1016/j.protis.2009.12.002. Epub 2010 Jan 13"