Phosphorylation-dephosphorylation of nuclear proteins during infection (Q fever).
The proposal that gene expression may be regulated by phosphorylation of nonhistone chromatin proteins was tested by studying increased transcription resulting from Q fever. Certain liver nuclear phosphoprotein kinase and phosphatase activities were altered after guinea pigs were infected with Coxiella burnetii. Nonhistone chromatin proteins had increased phosphoprotein kinase activity and were differentially phosphorylated. The addition of spermine equally stimulated nuclear phosphoprotein kinases of uninfected and infected livers. Increased nuclear phosphatase activity accompanied infection. It was concluded that protein phosphorylations are altered by infection and are central events in regulating RNA and protein synthesis. A hypothesis is presented which attempts to correlate the findings in previous reports and those in the present paper regarding biochemical sequelae of Q fever. It is suggested that certain features of regulation described here also may be operative in some other infections or diseases.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification / Q000378:metabolism*; D006168:Guinea Pigs; D008099:Liver / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011778:Q Fever / Q000378:metabolism*
D002868:Chromosomal Proteins, Non-Histone; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D000135:Acid Phosphatase