Identification and immunochemical location of UMP kinase from Bacillus subtilis

• Published in: Current microbiology 2004-01, Vol.48 (1), p.62-67
• Main Authors: Gagyi, Cristina, Ionescu, Mihaela, Gounon, Pierre, Sakamoto, Hiroshi, Rousselle, Jean-Claude, Laurent-Winter, Christine
• Format: Article
• Language: English
• Subjects: Bacillus subtilis; Bacillus subtilis - enzymology; Bacillus subtilis - ultrastructure; Bacteria; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Bacteriology; Blotting, Western; DNA, Bacterial - chemistry; DNA, Bacterial - genetics; E coli; Electrophoresis, Gel, Two-Dimensional; Guanosine Triphosphate - metabolism; Immunohistochemistry; Microscopy, Immunoelectron; Nucleoside-Phosphate Kinase - isolation & purification; Nucleoside-Phosphate Kinase - metabolism; Polymerase Chain Reaction
• ISSN: 0343-8651; 1432-0991
• DOI: 10.1007/s00284-003-4117-2

Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unstable in the absence of UTP, which acts as an allosteric inhibitor. Antibodies raised against recombinant B. subtilis UMP kinase recognized the protein both in soluble extract and in immunoelectron microscopy. UMP kinase from B. subtilis has a peripheral distribution which is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.