Abstract
The number, size and shape of polymorphic plant mitochondria are determined at least partially by mitochondrial fission. Arabidopsis mitochondria divide through the actions of a dynamin-related protein, DRP3A. Another plant-specific factor, ELM1, was previously shown to localize DRP3A to mitochondrial fission sites. Here, we report that mitochondrial fission is not completely blocked in the Arabidopsis elm1 mutant and that it is strongly manifested in response to cold treatment. Arabidopsis has an ELM1 paralogue (ELM2) that seems to have only a limited role in mitochondrial fission in the elm1 mutant. Interestingly, cold-induced mitochondrial fragmentation was also observed in the wild-type, but not in a drp3a mutant, suggesting that cold-induced transient mitochondrial fragmentation requires DRP3A but not ELM1 or ELM2. DRP3A: GFP localized from the cytosol to mitochondrial fission sites without ELM1 after cold treatment. Together, these results suggest that Arabidopsis has a novel, cold-induced type of mitochondrial fission in which DRP3A localizes to mitochondrial fission sites without the involvement of ELM1 or ELM2.
Highlights
Mitochondria are not made de novo but are created by fission of existing mitochondria [1]
Mitochondrial fission is mediated by a type of GTPase called dynamin-related proteins (DRPs), which are well conserved in eukaryotes [6,7,8,9]
DRPs polymerize into a ring-like spiral structure surrounding mitochondrial fission sites from the outer surface of mitochondria, and constrict to cleave the mitochondria by their GTPase activity [10,11,12,13]
Summary
Mitochondria are not made de novo but are created by fission of existing mitochondria [1]. Mitochondrial fission is mediated by a type of GTPase called dynamin-related proteins (DRPs), which are well conserved in eukaryotes [6,7,8,9]. DRPs polymerize into a ring-like spiral structure surrounding mitochondrial fission sites from the outer surface of mitochondria, and constrict to cleave the mitochondria by their GTPase activity [10,11,12,13]. DRP3A and DRP3B (formerly known as ADL2a and ADL2b), are most similar to mitochondrial fission-related DRPs in other eukaryotes [14,15]. In drp3a drp3b double mutants, mitocfhisosinodnritahaanre DfaRrPm3Bo.reIneloTn-DgNatAed,infoserrmtioinngmanutiannttesrcoofnDneRcPte3Ad naentdwoDrRkPi3nBea(cdhrp3cealla,nbdecdarups3eb)o, f the severmdeodiutoibsclrheuopmntduiortiananaotsrf,emmloiinttoogccehhrooannndddrirfaieawalrefiersfisanironmnuom[1reb9e]er.lothnagnattehdo,sfeoirnmtihneg wild type.
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