RRC ID 29670
著者 Fujiwara T, Kuroiwa H, Yagisawa F, Ohnuma M, Yoshida Y, Yoshida M, Nishida K, Misumi O, Watanabe S, Tanaka K, Kuroiwa T.
タイトル The coiled-coil protein VIG1 is essential for tethering vacuoles to mitochondria during vacuole inheritance of Cyanidioschyzon merolae.
ジャーナル Plant Cell
Abstract Vacuoles/lysosomes function in endocytosis and in storage and digestion of metabolites. These organelles are inherited by the daughter cells in eukaryotes. However, the mechanisms of this inheritance are poorly understood because the cells contain multiple vacuoles that behave randomly. The primitive red alga Cyanidioschyzon merolae has a minimum set of organelles. Here, we show that C. merolae contains about four vacuoles that are distributed equally between the daughter cells by binding to dividing mitochondria. Binding is mediated by VIG1, a 30-kD coiled-coil protein identified by microarray analyses and immunological assays. VIG1 appears on the surface of free vacuoles in the cytosol and then tethers the vacuoles to the mitochondria. The vacuoles are released from the mitochondrion in the daughter cells following VIG1 digestion. Suppression of VIG1 by antisense RNA disrupted the migration of vacuoles. Thus, VIG1 is essential for tethering vacuoles to mitochondria during vacuole inheritance in C. merolae.
巻・号 22(3)
ページ 772-81
公開日 2010-3-1
DOI 10.1105/tpc.109.070227
PII tpc.109.070227
PMID 20348431
PMC PMC2861457
MeSH Algal Proteins / genetics Algal Proteins / metabolism* Cell Cycle Gene Expression Profiling Microscopy, Electron, Transmission Mitochondria / metabolism* Rhodophyta / genetics* Rhodophyta / metabolism Sequence Analysis, Protein Vacuoles / metabolism* Vacuoles / ultrastructure
IF 9.618
引用数 18
WOS 分野 PLANT SCIENCES BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
リソース情報
藻類 NIES-3377