[Demonstration of 3 functional domains responsible for a kinase activity in VirA, a transmembrane sensory protein encoded by the Ti plasmid of Agrobacterium tumefaciens].
High-level expression of chimeric virA genes were obtained by replacing the first codons of virA with the first codons of trpE. The fusion proteins encoded by these constructs were partially purified and one of them exhibited autokinase activity. Therefore, protein phosphorylation may be an important feature of VirA function. This allowed us to define the existence of three functional domains inside VirA.
Morel
P
P
Department of Plant Pathology, University of California, Davis 95616.
Powell
B S
BS
Kado
C I
CI
D001426:Bacterial Proteins / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005827:Genetics, Microbial; D066298:In Vitro Techniques; D010957:Plasmids / Q000235:genetics; D011494:Protein Kinases / Q000235:genetics*; D012231:Rhizobium / Q000201:enzymology / Q000235:genetics*; D037521:Virulence Factors
D001426:Bacterial Proteins; D037521:Virulence Factors; D011494:Protein Kinases
Mise en évidence de trois domaines fonctionnels responsables d'une activité kinase chez VirA, une protéine sensorielle transmembranaire codée par le plasmide Ti d'Agrobacterium tumefaciens.