A spontaneous translational fusion of Bacillus cereus PlcR and PapR activates transcription of PlcR-dependent genes in Bacillus anthracis via binding with a specific palindromic sequence

Infection and Immunity
Andrei P PomerantsevStephen H Leppla

Abstract

Transformation of Bacillus anthracis with plasmid pUTE29-plcR-papR carrying the native Bacillus cereus plcR-papR gene cluster did not activate expression of B. anthracis hemolysin genes, even though these are expected to be responsive to activation by the global regulator PlcR. To further characterize the action of PlcR, we examined approximately 3,000 B. anthracis transformants containing pUTE29-plcR-papR and found a single hemolytic colony. The hemolytic strain contained a plasmid having a spontaneous plcR-papR intergenic region deletion. Transformation of the resulting plasmid pFP12, encoding a fused PlcR-PapR protein, into the nonhemolytic B. anthracis parental strain produced strong activation of B. anthracis hemolysins, including phosphatidylcholine-specific phospholipase C and sphingomyelinase. The fused PlcR-PapR protein present in a lysate of B. anthracis containing pFP12 bound strongly and specifically to the double-stranded palindrome 5'-TATGCATTATTTCATA-3' that matches the consensus PlcR-binding site. In contrast, native PlcR protein in a lysate from a B. anthracis strain expressing large amounts of this protein did not demonstrate binding with the palindrome. The results suggest that the activation of PlcR by bindi...Continue Reading

References

May 1, 1986·Infection and Immunity·B E IvinsS H Leppla
Aug 5, 1997·Proceedings of the National Academy of Sciences of the United States of America·M Perego
Jan 1, 1997·Annual Review of Microbiology·G M Dunny, B A Leonard
Mar 29, 2000·Protein Expression and Purification·S Park, S H Leppla
Dec 6, 2000·Genome Biology·N M LuscombeJ M Thornton
Dec 9, 2000·International Journal of Medical Microbiology : IJMM·D LereclusM Gominet
Oct 6, 2001·Peptides·M Perego, J A Brannigan
Nov 29, 2002·Frontiers in Bioscience : a Journal and Virtual Library·Mridula Pottathil, Beth A Lazazzera
Jul 26, 2003·Protein Expression and Purification·Joungmok KimMoon-Young Yoon

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Citations

Apr 6, 2005·FEMS Microbiology Reviews·David A RaskoJacques Ravel
Feb 12, 2008·Applied and Environmental Microbiology·Anirban Banerjee, Indranil Biswas
Sep 19, 2006·Journal of Bacteriology·Caná L Ross, Theresa M Koehler
Sep 5, 2008·PloS One·Pradeep K GuptaStephen H Leppla
Nov 14, 2007·Proceedings of the National Academy of Sciences of the United States of America·Nathalie DeclerckStefan T Arold
Aug 7, 2010·Microbiology·Inka SastallaStephen H Leppla
Jan 23, 2009·FEMS Immunology and Medical Microbiology·Andrei P PomerantsevStephen H Leppla
Feb 6, 2020·Biological & Pharmaceutical Bulletin·Masataka OdaGo Kamoshida

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