Full publication list for Rebecca Page .

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Wang, X., Kim, Y., Hong, S.H., Ma, Q., Brown, B.L., Pu, M. Tarone, A.M., Benedik, J.M., Peti, W., Page, R., Wood, T.K. (2011) Antitoxin MqsA helps mediate the bacterial general stress response. (2011) Nat Chem Biol (Epub ahead of print)

Brown, B.L., Wood, T.K., Peti, W., Page, R. (2011) Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation.. J Biol Chem 286:2285-96.

Recognized by the Faculty of 1000, Biology

Comeau, A.B., Critton, D.A., Page, R., Seto, C.T. (2010) A focused library of protien tyrosine phosphatase inhibitors. J Med Chem 53:6768-6772.

Ragusa, M.J., Dancheck, B., Critton, D.A., Nairn, A.C., Page, R., Peti, W. (2010) Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat Struct Mol Biol, 17, 459-464.

Critton, D.A., Tortajada, A., Stetson, G., Peti, W., Page, R. (2008) Structural basis of substrate recognition by Hematopoietic Tyrosine Phosphatase (HePTP). Biochem. 47, 13336-13345. Also selected as a highlighted article in Biochemistry.

Lee, J.*, Page, R.*, Contreras, R.G., Palermino, J.M., Zhang, X.S., Doshi, O., Wood, T.K. and Peti, W. (2007) Structure and function of the E. coli protein YMGB : a protein critical for biofilm formation and acid resistance. J Mol Biol, 373, 11-26. *These authors contributed equally to this work

Page, R.*, Peti, W.*, Wilson, I. A., Stevens, R. C., & Wüthrich, K. (2005) NMR screening and crystal quality of bacterial expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline. PNAS, 102, 1901-1905. *These authors contributed equally to this work

Canaves, J., Page, R., Wilson, I. A. & Stevens, R. C. (2004) Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics. J Mol Biol, 344, 977-991.

 

 

Although it is well recognized that bacteria respond to environmental stress through global networks, the mechanism by which stress is relayed to the interior of the cell is poorly understood. Here we show that enigmatic toxin-antitoxin systems are vital in mediating the environmental stress response. Specifically, the antitoxin MqsA represses rpoS, which encodes the master regulator of stress. Repression of rpoS by MqsA reduces the concentration of the internal messenger 3,5-cyclic diguanylic acid, leading to increased motility and decreased biofilm formation. Furthermore, the repression of rpoS by MqsA decreases oxidative stress resistance via catalase activity. Upon oxidative stress, MqsA is rapidly degraded by Lon protease, resulting in induction of rpoS. Hence, we show that external stress alters gene regulation controlled by toxin-antitoxin systems, such that the degradation of antitoxins during stress leads to a switch from the planktonic state (high motility) to the biofilm state (low motility).

From: Wang, X., Kim, Y., Hong, S.H., Ma, Q., Brown, B.L., Pu, M. Tarone, A.M., Benedik, J.M., Peti, W., Page, R., Wood, T.K. (2011) Antitoxin MqsA helps mediate the bacterial general stress response. (2011) Nat Chem Biol (Epub ahead of print)