[The splitting of the acceptor proteins of the protein kinase system in eukaryotic cells by Legionella cytolysin].
In the process of protein kinase reaction carried out in the mixture consisting of tris-HCl buffer, EDTA, MgCl2, gamma-32P-ATP and the cytoplasmic fraction of rabbit pulmonary cells the phosphorylation of proteins with molecular weights of 150 and 55 kD took place. The addition of L. pneumophila culture fluid to the reaction mixture resulted in the splitting of phosphorylated proteins with the formation of the component having a molecular weight of 45 kD. These disturbances in protein kinase reaction were found to occur due to the involvement of Legionella cytoplasm, a previously characterized protein with a molecular weight of 37 kD, into the process. In this connection, the participation of cytolysin in the pathogenesis of Legionella infection may also be considered from the viewpoint of the effect produced by cytolysin on the regulatory processes affecting the metabolism of target cells.
Belyĭ
Iu F
IuF
Tartakovskiĭ
I S
IS
Vertiev
Iu V
IuV
Prozorovskiĭ
S V
SV
D000818:Animals; D003600:Cytosol / Q000187:drug effects / Q000201:enzymology; D003603:Cytotoxins / Q000494:pharmacology*; D016952:Legionella pneumophila / Q000472:pathogenicity; D008168:Lung / Q000187:drug effects* / Q000201:enzymology; D008970:Molecular Weight; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000187:drug effects* / Q000378:metabolism; D011817:Rabbits; D013696:Temperature
D003603:Cytotoxins; D011494:Protein Kinases
Rasshcheplenie aktseptornykh belkov proteinkhinaznoĭ sistemy éukarioticheskikh kletok tsitolizinom legionell.