RRC ID 29670
Author Fujiwara T, Kuroiwa H, Yagisawa F, Ohnuma M, Yoshida Y, Yoshida M, Nishida K, Misumi O, Watanabe S, Tanaka K, Kuroiwa T.
Title The coiled-coil protein VIG1 is essential for tethering vacuoles to mitochondria during vacuole inheritance of Cyanidioschyzon merolae.
Journal 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.
Volume 22(3)
Pages 772-81
Published 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
Times Cited 18
Algae NIES-3377