Identification and immunochemical location of UMP kinase from Bacillus subtilis.
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.
Gagyi
Cristina
C
Laboratoire de Chimie Structurale des Macromolecules, Institut Pasteur, 75724 Paris Cedex 15, France. obarzu@pasteur.fr
Ionescu
Mihaela
M
Gounon
Pierre
P
Sakamoto
Hiroshi
H
Rousselle
Jean-Claude
JC
Laurent-Winter
Christine
C
D001412:Bacillus subtilis / Q000201:enzymology* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D015153:Blotting, Western; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D006160:Guanosine Triphosphate / Q000378:metabolism; D007150:Immunohistochemistry; D016253:Microscopy, Immunoelectron; D009703:Nucleoside-Phosphate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D016133:Polymerase Chain Reaction
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D006160:Guanosine Triphosphate; C023276:uridine monophosphate kinase; D009703:Nucleoside-Phosphate Kinase