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Chloroplast Ubiquitin E3 Ligase SP1: Does It Really Function in Peroxisomes?
Author(s) -
Qihua Ling,
Na Li,
Paul Jarvis
Publication year - 2017
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.17.00948
Subject(s) - ubiquitin ligase , chloroplast , ubiquitin , regulator , peroxisome , microbiology and biotechnology , proteasome , biology , dna ligase , chemistry , biochemistry , enzyme , gene
Pan et al. (2016) presented evidence that the plant ubiquitin E3 ligase SP1 directs proteasome-mediated regulation of the peroxisomal protein import machinery. This was surprising, as SP1 was originally identified as a chloroplast outer envelope-localized regulator of the chloroplast protein import machinery (Ling et al., 2012; Ling and Jarvis, 2015), and there was nothing in the original datasets to suggest functions elsewhere in the cell. It was also difficult to understand how a key regulator of chloroplast protein import, which mediates nuanced and selective effects during development and under stress (Ling et al., 2012; Ling and Jarvis, 2015), could additionally operate in a second organelle with a very different protein import system (Léon et al., 2006). We sought to address these issues by conducting additional experimental analyses

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