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Maciag, M, Kochanowska, M, Lyzeń, R, Wegrzyn, G and Szalewska-Pałasz, A (2010) ppGpp inhibits the activity of Escherichia coli DnaG primase. Plasmid 63:61-7


DNA primase is an enzyme required for replication of both chromosomes and vast majority of plasmids. Guanosine tetra- and penta-phosphate (ppGpp and pppGpp, respectively) are alarmones of the bacterial stringent response to starvation and stress conditions, and act by modulation of the RNA polymerase activity. Recent studies indicated that the primase-catalyzed reaction is also inhibited by (p)ppGpp in Bacillus subtilis, where a specific regulation of DNA replication elongation, the replication fork arrest, was discovered. Although in Escherichia coli such a replication regulation was not reported to date, here we show that E. coli DnaG primase is directly inhibited by ppGpp and pppGpp. However, contrary to the B. subtilis primase response to the stringent control alarmones, the E, coli DnaG was inhibited more efficiently by ppGpp than by pppGpp.


PubMed Online version:10.1016/j.plasmid.2009.11.002


Amino Acid Sequence; Bacillus subtilis/enzymology; DNA Primers/metabolism; DnaB Helicases/metabolism; Endodeoxyribonucleases/antagonists & inhibitors; Endodeoxyribonucleases/chemistry; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli Proteins/antagonists & inhibitors; Escherichia coli Proteins/chemistry; Exodeoxyribonucleases/antagonists & inhibitors; Exodeoxyribonucleases/chemistry; Guanosine Diphosphate/pharmacology; Guanosine Pentaphosphate/pharmacology; Guanosine Tetraphosphate/pharmacology; Models, Molecular; Molecular Sequence Data; Sequence Homology, Amino Acid


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