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Review
. 2014 Aug 14;10(8):e1004255.
doi: 10.1371/journal.ppat.1004255. eCollection 2014 Aug.

Hell's BELs: bacterial E3 ligases that exploit the eukaryotic ubiquitin machinery

Jon Huibregtse  1 , John R Rohde  2
Affiliations
Review

Hell's BELs: bacterial E3 ligases that exploit the eukaryotic ubiquitin machinery

Jon Huibregtse et al. PLoS Pathog. .
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Bacteria encode E3 ubiquitin ligases of many classes.
BELs share little or no sequence homology with eukaryotic E3s; however, structural similarities exist between BELs and eukaryotic E3s. Some BELs display entirely novel interactions with their cognate E2s. A. There are examples of bacterial E3 ligases that function similar to RING-type or HECT E3s in eukaryotic cells. Some BELs have novel mechanisms of ubiquitin transfer and interact with E2s in unique ways. B. Evidence exists for regulation of BEL activity inside eukaryotic cells. NEL domain enzymes are autoinhibited until they engage their substrates. AvrPtoB, a RING-type E3, can promote disease by ubiquitinating and causing degradation of the R proteins Pto and Fen (purple). Pto (brown) can also associate with AvrPtoB through an alternate domain allowing it to evade ubiquitination and initiating an ETI.
See this image and copyright information in PMC

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