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Identification and characterization of a putative arginine kinase in Myxococcus xanthus
Author(s) -
Naples Colin,
Fraga Dean
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a300
Subject(s) - myxococcus xanthus , arginine kinase , biology , biochemistry , kinase , gene , genetics , arginine , amino acid , mutant
Arginine kinases (AK) are members of the phosphagen kinase family and like other phosphagen kinases, they help in regulating energy metabolism in the cell. They catalyze the transfer of a high‐energy phosphoryl group between ATP and arginine in invertebrates and protozoa. A BLAST search conducted in June of 2006 revealed that the recently released genome sequence of Myxococcus xanthus contained a putative arginine kinase (AK) gene with high sequence identity to horseshoe crab AK (~48%). Phylogenetic analysis revealed that the catalytic domain of this protein sequence clusters with the catalytic domain of AKs found in protozoa and invertebrates. It does not cluster with an AK‐like sequence recently identified in Bacillus subtilis and other firmicutes that has been described to have tyrosine kinase activity. The purpose of this study is to determine if this putative AK does indeed have AK activity. The putative arginine kinase (AK) sequence encoded in the Myxococcus genome was amplified via PCR and cloned into the pMALc2g2 vector. A successful clone was identified and subsequently transformed in Rosetta BL21 cells for expression and characterization. We are currently in the process of purifying the protein for kinetic analysis. The results will be compared with an already characterized bacteria AK from Desulfotalea psychrophila LSv54 . This research was supported by NSF grant #0344432.