Chlamydomonas reinhardtii centrin is a member of the EF-hand calcium-binding superfamily. It is found in the basal body complex and is important for flagellar motility. Like other members of the EF-hand family, centrin interacts with and modulates the function of other proteins in a calcium-dependent manner. To understand how C. reinhardtii centrin interacts with its protein targets, it has been crystallized in the presence of the model peptide melittin and X-ray diffraction data have been collected to 2.2 A resolution. The crystals are orthorhombic, with unit-cell parameters a = 52.1, b = 114.4, c = 34.8 A, and are likely to belong to space group P2(1)2(1)2.
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http://dx.doi.org/10.1107/S1744309108009123 | DOI Listing |
Plant J
August 2024
MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Chlamydomonas reinhardtii, a unicellular green alga, has been widely used as a model organism for studies of algal, plant and ciliary biology. The generation of targeted amino acid mutations is often necessary, and this can be achieved using CRISPR/Cas9 induced homology-directed repair to install genomic modifications from exogenous donor DNA. Due to the low gene editing efficiency, the technical challenge lies in identifying the mutant cells.
View Article and Find Full Text PDFCells
July 2018
Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA.
During ciliogenesis, centrioles convert to membrane-docked basal bodies, which initiate the formation of cilia/flagella and template the nine doublet microtubules of the flagellar axoneme. The discovery that many human diseases and developmental disorders result from defects in flagella has fueled a strong interest in the analysis of flagellar assembly. Here, we will review the structure, function, and development of basal bodies in the unicellular green alga , a widely used model for the analysis of basal bodies and flagella.
View Article and Find Full Text PDFBiophys J
June 2017
Department of Chemistry, University of Puerto Rico Mayagüez Campus, Mayagüez, Puerto Rico; Protein Research Center, University of Puerto Rico Mayagüez Campus, Mayagüez, Puerto Rico. Electronic address:
Pre-mRNA processing protein 40 (Prp40) is a nuclear protein that has a role in pre-mRNA splicing. Prp40 possesses two leucine-rich nuclear export signals, but little is known about the function of Prp40 in the export process. Another protein that has a role in protein export is centrin, a member of the EF-hand superfamily of Ca-binding proteins.
View Article and Find Full Text PDFCilia
June 2016
University of Colorado at Boulder, Boulder, USA.
The unicellular green alga, Chlamydomonas reinhardtii, is a biflagellated cell that can swim or glide. C. reinhardtii cells are amenable to genetic, biochemical, proteomic, and microscopic analysis of its basal bodies.
View Article and Find Full Text PDFMicrob Cell
August 2014
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030, U.S.A.
Centrin is an evolutionarily conserved EF-hand calcium-binding protein found in the centriole of animals and the basal body of flagellated organisms. It was originally discovered in the flagellated unicellular green alga , where it associates with flagellum-associated structures and regulates basal body duplication and flagellar motility. Centrin constitutes a light chain of three inner-arm dynein complexes in the flagellar axoneme in , and presumably regulates the activity of the inner-arm dynein for flagellar motility.
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