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https://doi.org/10.1371/journal.pone.0019720
Title: | Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination | Authors: | Chew, K.C.M. Matsuda, N. Saisho, K. Lim, G.G.Y. Chai, C. Tan, H.-M. Tanaka, K. Lim, K.-L. |
Issue Date: | 2011 | Citation: | Chew, K.C.M., Matsuda, N., Saisho, K., Lim, G.G.Y., Chai, C., Tan, H.-M., Tanaka, K., Lim, K.-L. (2011). Parkin mediates apparent E2-independent monoubiquitination in vitro and contains an intrinsic activity that catalyzes polyubiquitination. PLoS ONE 6 (5) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0019720 | Abstract: | Background: Mutations in the parkin gene, which encodes a ubiquitin ligase (E3), are a major cause of autosomal recessive parkinsonism. Although parkin-mediated ubiquitination was initially linked to protein degradation, accumulating evidence suggests that the enzyme is capable of catalyzing multiple forms of ubiquitin modifications including monoubiquitination, K48- and K63-linked polyubiquitination. In this study, we sought to understand how a single enzyme could exhibit such multifunctional catalytic properties. Methods and Findings: By means of in vitro ubiquitination assays coupled with mass spectrometry analysis, we were surprised to find that parkin is apparently capable of mediating E2-independent protein ubiquitination in vitro, an unprecedented activity exhibited by an E3 member. Interestingly, whereas full length parkin catalyzes solely monoubiquitination regardless of the presence or absence of E2, a truncated parkin mutant containing only the catalytic moiety supports both E2-independent and E2-dependent assembly of ubiquitin chains. Conclusions: Our results here suggest a complex regulation of parkin's activity and may help to explain how a single enzyme like parkin could mediate diverse forms of ubiquitination. © 2011 Chew et al. | Source Title: | PLoS ONE | URI: | http://scholarbank.nus.edu.sg/handle/10635/109508 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0019720 |
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