Identification of a Novel Leucine-rich Repeat Protein as a Component of Flagellar Radial Spoke in the Ascidian Ciona intestinalis. Padma, P., Satouh, Y., Wakabayashi, K., Hozumi, A., Ushimaru, Y., Kamiya, R., & Inaba, K. Molecular Biology of the Cell, 14(2):774–785, November, 2002. Publisher: American Society for Cell Biology (mboc)![Identification of a Novel Leucine-rich Repeat Protein as a Component of Flagellar Radial Spoke in the Ascidian Ciona intestinalis [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Axonemes are highly organized microtubule-based structures conserved in many eukaryotes. In an attempt to study axonemes by a proteomics approach, we selectively cloned cDNAs of axonemal proteins by immunoscreening the testis cDNA library from the ascidianCiona intestinalis by using an antiserum against whole axonemes. We report here a 37-kDa protein of which cDNA occurred most frequently among total positive clones. This protein, named LRR37, belongs to the class of SDS22+ leucine-rich repeat (LRR) family. LRR37 is different from the LRR outer arm dynein light chain reported inChlamydomonas and sea urchin flagella, and thus represents a novel axonemal LRR protein. Immunoelectron microscopy by using a polyclonal antibody against LRR37 showed that it is localized on the tip of the radial spoke, most likely on the spoke head. The LRR37 protein in fact seems to form a complex together with radial spoke protein 3 in a KI extract of the axonemes. These results suggest that LRR37 is a component of the radial spoke head and is involved in the interaction with other radial spoke components or proteins in the central pair projection.
@article{padma_identification_2002,
title = {Identification of a {Novel} {Leucine}-rich {Repeat} {Protein} as a {Component} of {Flagellar} {Radial} {Spoke} in the {Ascidian} {Ciona} intestinalis},
volume = {14},
issn = {1059-1524},
url = {https://www.molbiolcell.org/doi/10.1091/mbc.02-06-0089},
doi = {10.1091/mbc.02-06-0089},
abstract = {Axonemes are highly organized microtubule-based structures conserved in many eukaryotes. In an attempt to study axonemes by a proteomics approach, we selectively cloned cDNAs of axonemal proteins by immunoscreening the testis cDNA library from the ascidianCiona intestinalis by using an antiserum against whole axonemes. We report here a 37-kDa protein of which cDNA occurred most frequently among total positive clones. This protein, named LRR37, belongs to the class of SDS22+ leucine-rich repeat (LRR) family. LRR37 is different from the LRR outer arm dynein light chain reported inChlamydomonas and sea urchin flagella, and thus represents a novel axonemal LRR protein. Immunoelectron microscopy by using a polyclonal antibody against LRR37 showed that it is localized on the tip of the radial spoke, most likely on the spoke head. The LRR37 protein in fact seems to form a complex together with radial spoke protein 3 in a KI extract of the axonemes. These results suggest that LRR37 is a component of the radial spoke head and is involved in the interaction with other radial spoke components or proteins in the central pair projection.},
number = {2},
urldate = {2020-03-03},
journal = {Molecular Biology of the Cell},
author = {Padma, Potturi and Satouh, Yuhkoh and Wakabayashi, Ken-ichi and Hozumi, Akiko and Ushimaru, Yuji and Kamiya, Ritsu and Inaba, Kazuo},
month = nov,
year = {2002},
note = {Publisher: American Society for Cell Biology (mboc)},
keywords = {Inaba K},
pages = {774--785}
}
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We report here a 37-kDa protein of which cDNA occurred most frequently among total positive clones. This protein, named LRR37, belongs to the class of SDS22+ leucine-rich repeat (LRR) family. LRR37 is different from the LRR outer arm dynein light chain reported inChlamydomonas and sea urchin flagella, and thus represents a novel axonemal LRR protein. Immunoelectron microscopy by using a polyclonal antibody against LRR37 showed that it is localized on the tip of the radial spoke, most likely on the spoke head. The LRR37 protein in fact seems to form a complex together with radial spoke protein 3 in a KI extract of the axonemes. 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