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Wataru Sakamoto

Researcher at Okayama University

Publications -  175
Citations -  6754

Wataru Sakamoto is an academic researcher from Okayama University. The author has contributed to research in topics: Chloroplast & Arabidopsis. The author has an hindex of 47, co-authored 164 publications receiving 5863 citations. Previous affiliations of Wataru Sakamoto include University of Tokyo & Boyce Thompson Institute for Plant Research.

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Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

TL;DR: It is concluded that VAR1 and VAR2 are the major components of an FtsH complex involved in the repair of photodamaged proteins in thylakoid membranes.
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Protein Degradation Machineries in Plastids

TL;DR: This review covers what is currently known about the types and function of plastid proteases together with new observations about the differential roles of these isomers in Arabidopsis.
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The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles.

TL;DR: Genetic analysis of the var1 mutant of Arabidopsis indicated that it acts synergistically with another mutation var2, suggesting that the two genes are relevant and possibly involved in the degradation of thylakoid proteins and plastid development.
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Widespread Endogenization of Genome Sequences of Non-Retroviral RNA Viruses into Plant Genomes

TL;DR: It is shown that single- and double-stranded RNA viral sequences are widespread in plant genomes, and the potential of genome integrated NRVSs to contribute to resolve unclear phylogenetic relationships of plant species is shown.
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Highly Oxidized Peroxisomes Are Selectively Degraded via Autophagy in Arabidopsis

TL;DR: It is demonstrated that hydrogen peroxide as a result of catalase inactivation is the inducer of peroxisome aggregation, and an autophagosome marker, ATG8, frequently colocalized with per oxisome aggregates, indicating thatPeroxisomes damaged by hydrogen per oxygen are selectively degraded by autophagy in the wild type.