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CmDnm1, in vitro phosphorylation by CmAUR, Gel

ABSTRACT: Recombinant Cyanidioschyzon Dnm1 protein (CmDnm1) was incubated with or without recombinant Cyanidioschyzon Aurora kinase (CmAUR). Proteins were separated by SDS-PAGE, in-gel tryptic digested, analyzed by LC-MS.

ORGANISM(S): Cellular Organisms

SUBMITTER: Hirofumi Nakagami

PROVIDER: PXD012329 | JPOST Repository | Tue Jan 14 00:00:00 GMT 2020

REPOSITORIES: jPOST

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			Action	DRS
	CmAUR_Dnm1.raw	Raw
	Dnm1.raw	Raw
	F021879.dat	Other
	F021882.dat	Other

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Publications

Cyanidioschyzon merolae aurora kinase phosphorylates evolutionarily conserved sites on its target to regulate mitochondrial division.

Kato Shoichi S Okamura Erika E Matsunaga Tomoko M TM Nakayama Minami M Kawanishi Yuki Y Ichinose Takako T Iwane Atsuko H AH Sakamoto Takuya T Imoto Yuuta Y Ohnuma Mio M Nomura Yuko Y Nakagami Hirofumi H Kuroiwa Haruko H Kuroiwa Tsuneyoshi T Matsunaga Sachihiro S

Communications biology 20191220

The mitochondrion is an organelle that was derived from an endosymbiosis. Although regulation of mitochondrial growth by the host cell is necessary for the maintenance of mitochondria, it is unclear how this regulatory mechanism was acquired. To address this, we studied the primitive unicellular red alga Cyanidioschyzon merolae, which has the simplest eukaryotic genome and a single mitochondrion. Here we show that the C. merolae Aurora kinase ortholog CmAUR regulates mitochondrial ...[more]

PMID: 31886415

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