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Classification of tyrosine kinases from Dictyostelium discoideum with two distinct, complete or incomplete catalytic domains
Author(s) -
Adler Kristin,
Gerisch Günther,
von Hugo Ulrike,
Lupas Andrei,
Schweiger Anton
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01053-8
Subject(s) - dictyostelium discoideum , kinase , dictyostelium , receptor tyrosine kinase , chemistry , tyrosine kinase , microbiology and biotechnology , mycetozoa , tyrosine , biochemistry , catalysis , biology , receptor , gene
Two new kinases of Dictyostelium discoideum were identified by screening of a λgt11 expression library with a phosphotyrosine specific antibody. Amino‐acid sequences derived from cDNA and genomic clones indicate that DPYK3 is a protein of 150 kDa and DPYK4, a protein of 75 kDa. The C‐terminal fragments of each protein were produced in Escherichia coli and shown to be autocatalytically phosphorylated at tyrosine residues. A common feature of these kinases is the presence of two different sequence stretches in tandem that are related to kinase catalytic domains. The sequence relationships of DPYK3 and 4 to other protein kinases, and the positions of their catalytic domain sequences within the phylogenetic tree of protein kinases were analysed. Domains I of both kinases and domain II of DPYK3 constitute, together with the catalytic domains of two previously described tyrosine kinases of D. discoideum , a branch of their own, separate from the tyrosine kinase domains in sensu strictu. Domain II in DPYK4 is found on a different branch close to serine/threonine kinases.