Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli

被引：43

作者：

Cerda-Maira, Francisca A. ^{[1
]}

McAllister, Fiona ^{[2
]}

Bode, Nadine J. ^{[1
]}

Burns, Kristin E. ^{[1
]}

Gygi, Steven P. ^{[2
]}

Darwin, K. Heran ^{[1
]}

机构：

[1] NYU, Sch Med, Dept Microbiol, New York, NY 10016 USA

[2] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

来源：

EMBO REPORTS | 2011年 / 12卷 / 08期

基金：

美国国家卫生研究院;

关键词：

Pup; Mycobacterium tuberculosis; proteasome; pupylation; UBIQUITIN-LIKE PROTEIN; PROTEASOME; PUP; PHOSPHORYLATION; IDENTIFICATION; TARGETS; LIGASES; MTFABD; DOP;

D O I：

10.1038/embor.2011.109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：863 / 870

页数：8

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