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regulation of gene expression

post translational modiFICation
by

Dilya Ibrasheva

on 23 April 2010

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Transcript of regulation of gene expression

Post-translational modiFICation

Dilya Ibrasheva


Large fibrillar surface antigen that is produced by the respiratory pathogen Histophilus somni and has been implicated in virulence and host toxicity. One section of IpbA is similar to Yopt, a known cytotoxic effector, while another one resembles filamentous hemaglutinin, which mediates attachment to host cells.






These proteins are a new class of post-translational modifying enzymes that add AMP to Rho-family of GTPases, thus regulating both bacterial pathogenesis and eukaryotic signalling
Fic domain-containing proteins are a novel class of enzymes that can both regulate prokaryotic pathogenesis and carry out previously unknown eukaryotic post-translational modification What do they do? IbpA Conclusion Reference: Worby, C. A. et al. The Fic domain: regulation of cell signaling by adenylylation. Mol.Cell 34, 93-103 (2009)
Huntingtin yeast- interacting protein E (HYPE), the only Fic-domain containing protein in humans, is also capable of adding AMP to RhoA, Rac, and CDC42. The Fic domains (containing fusion proteins) are responsible for disruption of the host actin cytoskeleton
Alignment of the Fic domain containing proteins revealed a common consensus sequence of HPFxxGNGR
Point mutation studies showed that one highly conserved residue H3717 represents a critical catalytic residue for Fic activity

Expression of Fic inhibits RhoA and Rac from binding to their downstream effectors
Fic adds an AMP moiety to a Tyr residue in RhoA, Rac, and Cdc42
Fic uses ATP to adenylylate RhoA, Rac, and Cdc42
This modification is reversible


Fic Domain HYPE Proteins Fic domain-containing proteins that are present in both eukaryotes and prokaryotes
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