Pathogen Puts a Spanner in the Works

Science's STKE  30 May 2006:
Vol. 2006, Issue 337, pp. tw181
DOI: 10.1126/stke.3372006tw181

So-called bacterial effector proteins usurp or mimic a eukaryotic activity and contribute to virulence. Many of the known virulence factors from the pathogenic bacterium Yersinia pestis, the causal agent of plague, have been assigned mechanisms, but YopJ has remained a mystery. Mukherjee et al. (see the Perspective by Worby and Dixon) now show that YopJ acts as an acetyltransferase that modifies serine or threonine residues in the activation loop of the MKK superfamily of signaling kinases. This modification prevents these residues from being phosphorylated by upstream signaling machinery and interferes with innate immune responses.

S. Mukherjee, G. Keitany, Y. Li, Y. Wang, H. L. Ball, E. J. Goldsmith, K. Orth, Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312, 1211-1214 (2006). [Abstract] [Full Text]

C. A. Worby, J. E. Dixon, Bacteria seize control by acetylating host proteins. Science 312, 1150-1151 (2006). [Summary] [Full Text]