Sequence and biochemical analysis of Arabidopsis SP1 protein, a regulator of organelle biogenesis

ABSTRACT

Peroxisomes, chloroplasts, and mitochondria are essential eukaryotic organelles that host a suite of metabolic processes crucial to energy metabolism and development. Regulatory mechanisms of the dynamics and biogenesis of these important organelles have begun to be discovered in plants. We recently showed that, aside from its previously reported role in targeting chloroplast protein import proteins, the Arabidopsis ubiquitin E3 ligase SP1 (suppressor of ppi1 locus1) negatively regulates peroxisome matrix protein import by promoting the ubiquitination and destabilization of PEX13 and possibly PEX14 and other components of the peroxisome protein import apparatus. Here, we compared protein sequence and domain structure of SP1-like proteins in Arabidopsis and their human homolog, Mitochondrial-Anchored Protein Ligase (MAPL). We further characterized SP1 protein in respect to its membrane topology and ubiquitin E3 ligase activity.

KEYWORDS:

• chloroplasts
• E3 ubiquitin ligase
• MAPL
• mitochondria
• peroxisomes
• SP1
• SPL1

Disclosure of potential conflicts of interest

No potential conflicts of interest were disclosed.

Acknowledgments

We thank Dr. Navneet Kaur for technical help.

Funding

This work was supported by the National Science Foundation (MCB 1330441) to J.H.