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Lupus is an autoimmune disease in which the body harms its own healthy cells. This leads to inflammation and damage to various tissues. In one form of the disease, known as systemic lupus erythematosus, patients produce antibodies against highly conserved RNA-binding proteins called Ro and La. As reported in the April issue of Nature Structural & Molecular Biology, the structure of the La protein shows how it binds to RNA. These studies suggest how an RNA-binding protein such as La may be involved in the autoimmune response.
Within the cell, La is one of the first proteins to bind many newly made RNAs. A major function of this protein is to protect these RNAs from being destroyed. Recent studies have shown that binding of La protein to some RNAs facilitates formation of their correctly folded structure. Now, Maria Conte and colleagues determine the NMR structures of two parts of the La protein, known as the La domain and the central RNA recognition motif (RRM). These structures show that the La domain has a distinct positive surface. This interacts with a similar surface on the RRM domain to bind RNA. Understanding how La protein interacts with RNA will facilitate studies of how this protein functions in cellular quality control mechanisms, which sequester and refold RNA molecules so that they do not interfere with normal cellular processes. The buildup of misfolded proteins and RNAs in the cell is thought to trigger autoimmune responses. In an autoimmune disorder such as lupus, the immune system loses its ability to discriminate between foreign substances and makes antibodies against itself (auto-antibodies). These antibodies react with 'self' antigens to form immune complexes, which build up in the tissues and cause inflammation and pain. Proteins such as La, that help fold and protect RNAs, may function to clear the cell of "self" antigens and thereby prevent an autoimmune response. Author contact:
Maria Rosaria Conte
University of Portsmouth, UK
Tel: +44 2392 842080
E-mail: sasi.conte@port.ac.uk
Additional contacts for comment on paper:
Jack D. Keene
Duke University Medical Center
Durham, NC
USA
Tel: +1 919 684 5138
E-mail: keene001@mc.duke.edu Daniel J. Kenan
Duke University Medical Center
Durham, NC
USA
Tel: +1 919 684 3300
E-mail: kenan001@mc.duke.edu Also available online. (C) Nature Structural & Molecular Biology press release.
Message posted by: Trevor M. D'Souza
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