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the capping domain in ralf regulates effector functions拉尔夫的覆盖域调节效应的功能
The Capping Domain in RalF Regulates Effector Functions 1 1 2 3 4¤ 4 Eric Alix *, Laurent Chesnel , Brad J. Bowzard , Aimee M. Tucker , Anna Delprato , Jacqueline Cherfils , 3 2 1 David O. Wood , Richard A. Kahn , Craig R. Roy 1 Department of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, Connecticut, United States of America, 2 Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America, 3 Department of Microbiology and Immunology, University of South Alabama, Mobile, Alabama, United States of America, 4 Laboratoire d’Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, CNRS Bat 34, CNRS, Gif sur Yvette, France Abstract The Legionella pneumophila effector protein RalF functions as a guanine nucleotide exchange factor (GEF) that activates the host small GTPase protein ADP-ribosylation factor (Arf), and recruits this host protein to the vacuoles in which this pathogen resides. GEF activity is conferred by the Sec7 domain located in the N-terminal region of RalF. Structural studies indicate that the C-terminal region of RalF makes contacts with residues in the Sec7 domain important for Arf interactions. Theoretically, the C-terminal region of RalF could prevent nucleotide exchange activity by blocking the ability of Arf to interact with the Sec7 domain. For this reason, the C-terminal region of RalF has been termed a capping domain. Here, the role of the RalF capping domain was investigated by comparing biochemical and effector activities mediated by this domain in both the Legionella RalF
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