The link between DNA methylation

and ribosome biosynthesis could be at the heart of the interaction between a Bleomycin solubility dmso host and a parasitic R-M system. As a large number of DNA methyltransferases found in REBASE modify 5′CCWGG3′sites, it is possible that R-M systems influence expression of ribosomal protein genes and/or other genes to promote their maintenance. The effect of Dcm and other DNA methyltransferases on the entire E. coli transcriptome is currently under investigation. We thank Dr John Crane (SUNY Buffalo) and Dr Martin Marinus (University of Massachusetts Medical School) for providing E. coli strains. We thank Dr Ashok Bhagwat (Wayne State University) for providing the pDcm-9 and pDcm-21 plasmids.

We thank Ping Wang and Joshua Prey at the Roswell Park Cancer Institute for the LC MS/MS analysis. Support for this work was provided by the Geneseo Foundation and NIH Grant R15AI074035-01 (K.T.M). K.T.M. and R.D.S. contributed equally to the work. Please note: Wiley-Blackwell is not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“The type III secretion system (T3SS) is a sophisticated protein secretion machinery that delivers bacterial virulence proteins into host Trichostatin A cost cells. A needle-tip protein, Bsp22, is one of the secreted substrates of the T3SS and plays an essential role in the full function of the T3SS in Bordetella bronchiseptica. In this study, we found that BB1618 functions as a chaperone for Bsp22. The deletion of BB1618 resulted in a dramatic impairment of Bsp22 secretion into the culture supernatants and Bsp22 stability in the bacterial cytosol. In contrast, the secretion of other type III secreted proteins was not affected by the BB1618 mutation. Furthermore, the BB1618 mutant strain could not induce cytotoxicity

and displayed the same phenotypes as the Bsp22 mutant strain. An immunoprecipitation assay demonstrated that BB1618 interacts with Bsp22, but not with BopB and BopD. Thus, we identified BB1618 as a specific type III chaperone for Bsp22. Therefore, we PI-1840 propose that BB1618 be renamed Btc22 for the Bordetella type III chaperone for Bsp22. Bordetella bronchiseptica is thought to be an evolutionary progenitor of Bordetella pertussis and Bordetella parapertussis, which are causative agents of whooping cough (pertussis) in humans (Mattoo & Cherry, 2005). Bordetella species produce and secrete many virulence factors, such as adhesins, toxins, and secreted proteins, via a type III secretion system (T3SS; Abe et al., 2008). The T3SS is a needle-like structure protruding from the bacterial surface and is required to exert full virulence in many Gram-negative pathogens, including Bordetella species (Abe et al., 2008).