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EMBO Rep. 2011 Jul 8;12(8):863-70. doi: 10.1038/embor.2011.109.

Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.

Author information

1
Department of Microbiology, New York University School of Medicine, 550 First Avenue, MSB 236, New York, New York 10016, USA.

Abstract

Prokaryotic ubiquitin-like protein (Pup) is a post-translational modifier that attaches to more than 50 proteins in Mycobacteria. Proteasome accessory factor A (PafA) is responsible for Pup conjugation to substrates, but the manner in which proteins are selected for pupylation is unknown. To address this issue, we reconstituted the pupylation of model Mycobacterium proteasome substrates in Escherichia coli, which does not encode Pup or PafA. Surprisingly, Pup and PafA were sufficient to pupylate at least 51 E. coli proteins in addition to the mycobacterial proteins. These data suggest that pupylation signals are intrinsic to targeted proteins and might not require Mycobacterium-specific cofactors for substrate recognition by PafA in vivo.

PMID:
21738222
PMCID:
PMC3147258
DOI:
10.1038/embor.2011.109
[Indexed for MEDLINE]
Free PMC Article

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