title: Protein Modification: Bacterial Effectors Rewrite the Rules of Ubiquitylation.
abstract: A family of virulence factors from the bacterial pathogen Legionella pneumophila has been discovered to modify human Rab GTPases with ubiquitin. Surprisingly, this modification occurs via a non-canonical mechanism that uses nicotinamide adenine dinucleotide as a cofactor.
authors.affiliation: Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.
authors.forename: Jason M
authors.initials: JM
authors.lastname: Berk
authors.affiliation: Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA. Electronic address: mark.hochstrasser@yale.edu.
authors.forename: Mark
authors.initials: M
authors.lastname: Hochstrasser
mesh_terms: D054884:Host-Pathogen Interactions; D006801:Humans; D016952:Legionella pneumophila / Q000302:isolation & purification / Q000378:metabolism / Q000472:pathogenicity*; D007877:Legionnaires' Disease / Q000201:enzymology* / Q000382:microbiology*; D009243:NAD / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D025801:Ubiquitin / Q000378:metabolism*; D054875:Ubiquitination; D037521:Virulence Factors / Q000378:metabolism*; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D037521:Virulence Factors; D009243:NAD; D020691:rab GTP-Binding Proteins