Editors' ChoiceMicrobiology

Mysterious Resistance Revealed

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Science's STKE  13 Mar 2001:
Vol. 2001, Issue 73, pp. tw6
DOI: 10.1126/stke.2001.73.tw6

Resistance against the penicillin family of antibiotics has almost become universal among clinically important strains of staphylococcal bacteria. When penicillin binds to a sensor on the surface of bacteria, a signal is transmitted across the cell membrane to cause removal of a DNA repressor protein and to allow the transcription of the various regulatory genes for expression of β-lactamase or of low-affinity penicillin-binding protein substitutes. Zhang et al. now show that penicillin binding to the sensor triggers self-proteolysis. The cleavage product then binds, either directly or via intermediates, to the DNA-binding repressor protein. The repression is lifted in a second proteolytic step when the DNA-binding protein is released and transcription of the antibiotic-resistance genes starts. For more details see the Perspective by Archer and Bosilevac.

H. Z. Zhang, C. J. Hackbarth, K. M. Chansky, H. F. Chambers, A proteolytic transmembrane signaling pathway and resistance to β-lactams in Staphylococci. Science 291, 1962-1965 (2001). [Abstract] [Full Text]

G. L. Archer, J. M. Bosilevac, Signaling antibiotic resistance in Staphylococci. Science 291, 1915-1916 (2001). [Full Text]

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