Three Uev1s Promote Ubc13-Mediated Lys63-Linked Polyubiquitination and Confer Different Functions.

Front Plant Sci

College of Life Sciences, Capital Normal UniversityBeijing, China; Department of Microbiology and Immunology, University of Saskatchewan, SaskatoonSK, Canada.

Published: October 2016

In this study, we report the identification and functional characterization of three genes. All three BdUev1s form heterodimers with BdUbc13s, which are capable of catalyzing Lys63-linked polyubiquitination . The three genes are also able to functionally complement the budding yeast mutant defective in DNA-damage tolerance. BdUev1A differs from the other two BdUev1s in that it contains an 18-amino acid tail, which appears to compromise its function in yeast, as deletion of this tail restores full function. BdUev1A is excluded from the nucleus, whereas BdUev1B, BdUev1C and the C-terminally truncated BdUev1A are mainly found in the nucleus. These and the gene expression analysis allow us to speculate that although all three BdUev1s function by promoting Lys63-linked polyubiquitination, BdUev1B and BdUev1C are involved in DNA-damage response and possibly other nuclear functions, while BdUev1A is required for non-nuclear function(s).

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5067413PMC
http://dx.doi.org/10.3389/fpls.2016.01551DOI Listing

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