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. 1984 Jan;43(1):14–20. doi: 10.1128/iai.43.1.14-20.1984

Phosphorylation-dephosphorylation of nuclear proteins during infection (Q fever).

F R Gonzales, M Halevy, D Paretsky
PMCID: PMC263380  PMID: 6317563

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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