title: Fluorescent probes reveal a minimal ligase recognition motif in the prokaryotic ubiquitin-like protein from Mycobacterium tuberculosis.
abstract: The prokaryotic ubiquitin-like protein (Pup)-based proteasomal system in the pathogen  Mycobacterium tuberculosis  (Mtb) is essential for its survival in a mammalian host. The Pup ligase enzyme, PafA, conjugates Pup to a suite of proteins targeted for proteasomal degradation and is necessary for persistent infection by Mtb. We report the design and application of fluorescent probes for use in elucidating the mechanisms of Pup and substrate recognition by PafA. Our studies revealed that the C-terminal 26 amino acid sequence of Pup is the minimal ligase recognition motif in Mtb. Specific hydrophobic residues within this sequence that are known to be important for the interactions of Pup with proteasomes are also critical for the activation of Pup by PafA.
authors: Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
authors: Denis
authors: D
authors: Smirnov
authors: Abhinav
authors: A
authors: Dhall
authors: Kalkena
authors: K
authors: Sivanesam
authors: Rudy J
authors: RJ
authors: Sharar
authors: Champak
authors: C
authors: Chatterjee
mesh_terms: D005456:Fluorescent Dyes / Q000737:chemistry*; D008025:Ligases / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D005456:Fluorescent Dyes; D025801:Ubiquitin; D008025:Ligases
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