Mutations in PIH proteins MOT48, TWI1 and PF13 define common and unique steps for preassembly of each, different ciliary dynein

• Type of Material: Article
• Authors: Ryosuke Yamamoto, Osaka University; Shiho Yanagi, Osaka University; Masahito Nagao, Osaka University; Yuya Yamasaki, Osaka University; Yui Tanaka, Osaka University; Winfield Sale, Emory University; Toshiki Yagi, Prefectural University of Hiroshima; Takahide Kon, Osaka University
• Language: English
• Date: 2020-11-01
• Publisher: Public Library Science
• Publication Version: Final Published Version
• Copyright Statement: © 2020 Yamamoto et al.
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1371/journal.pgen.1009126
• Title of Journal or Parent Work: PLoS Genetics
• Volume: 16
• Issue: 11
• Start Page: e1009126
• End Page: e1009126
• Grant/Funding Information: National Institutes of Health Grant R01 (GM051173)(https://www.nih.gov)(to WSS); JSPS Grant-in-Aid for Young Scientists (B)(JP17K15117) and for Scientific Research (C)(JP20K06622)(https://www.jsps.go.jp/)(to RY); JSPS Grant-in-Aid for Scientific Research (B)(JP26291034 and JP17H03665)(https://www.jsps.go.jp/)(to TK).; JSPS Grant-in-Aid for Scientific Research (C)(JP26440074)(https://www.jsps.go.jp/) and MEXT Grant-in-Aid for Scientific Research on Innovative Areas (JP15H01327)(https://www.mext.go.jp/)(to TY); Ito Chubei Foundation (https://www.chubei-foundation.or.jp/); This study was partially funded by grants from the Uehara Memorial Foundation (https://www.ueharazaidan.or.jp/)
• Keywords: Outer; Science & Technology; Genetics & Heredity; Mutant; Axonemal; Life Sciences & Biomedicine; Flagella; Subunit; Complex; Purification; Genetics; Chlamydomonas-reinhardtii; Inner-arm dynein
• Research Categories: Biology, Genetics; Biology, Cell; Environmental Sciences

Abstract

Ciliary dyneins are preassembled in the cytoplasm before being transported into cilia, and a family of proteins containing the PIH1 domain, PIH proteins, are involved in the assembly process. However, the functional differences and relationships between members of this family of proteins remain largely unknown. Using Chlamydomonas reinhardtii as a model, we isolated and characterized two novel Chlamydomonas PIH preassembly mutants, mot48-2 and twi1-1. A new allele of mot48 (ida10), mot48-2, shows large defects in ciliary dynein assembly in the axoneme and altered motility. A second mutant, twi1-1, shows comparatively smaller defects in motility and dynein assembly. A double mutant mot48-2; twi1-1 displays greater reduction in motility and in dynein assembly compared to each single mutant. Similarly, a double mutant twi1-1; pf13 also shows a significantly greater defect in motility and dynein assembly than either parent mutant. Thus, MOT48 (IDA10), TWI1 and PF13 may define different steps, and have partially overlapping functions, in a pathway required for ciliary dynein preassembly. Together, our data suggest the three PIH proteins function in preassembly steps that are both common and unique for different ciliary dyneins.