PDF(1187 KB)
Protein Phosphatase 2CInvolved in the Flagellar Transition Zone Structure of Chlamydomonas reinhardtii
HE Wei, PAN Jun-min
China Biotechnology ›› 2016, Vol. 36 ›› Issue (5) : 68-73.
PDF(1187 KB)
PDF(1187 KB)
Protein Phosphatase 2CInvolved in the Flagellar Transition Zone Structure of Chlamydomonas reinhardtii
Objective:Using insertional mutagenesis in Chlamydomonas to identify genes required for flagellar assembly, so as to researching the function of the gene related to flagellar assembly. Methods:By transforming the DNA fragment harboring paromomycinresistance gene into Chlamydomonas randomly, the mutant strainwith flagellar defect is obtained and identified the disrupted gene was CrPP2C(Chlamydomonas reinhardtii type 2C protein phosphatase).Then the CrPP2C gene function is analyzed by biochemistry methods. Results:Theflagella abnormal mutantsthat show short flagella or none flagella are obtained by electroporation transformation.DNA sequence analysis show that the CrPP2C gene is disrupted. Transformation of mutants with CrPP2C-HA could rescue the flagellar phenotype.The mutants could regenerateflagella to the original length and shorte normally. Electron microscopyimages show incomplete Y-link structure in the transition zone of flagella. Conclusion:The CrPP2C gene is associated with the transition zone structure and affects the assembly of flagella.
Flagellar transition zone / Chlamydomonas reinhardtii / CrPP2C {{custom_keyword}} /
[1] Muqing C, Junmin P. Cilia and ciliopathies. Chinese Journal of Cell Biology, 2012, 34(9): 849-856.
[2] Chih B, Liu P, Chinn Y, et al. A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain. Nature Cell Biology, 2012, 14(1): 61-72.
[3] Czarnecki P G, Shah J V. The ciliary transition zone: from morphology and molecules to medicine. Trends in Cell Biology, 2012, 22(4): 201-210.
[4] Garcia-Gonzalo F R, Corbit K C, Sirerol-Piquer M S, et al. A transition zone complex regulates mammalian ciliogenesis and ciliary membrane composition. Nature Genetics, 2011, 43(8): 776-784.
[5] Lambacher N J, Bruel A L, van Dam T J P, et al. TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome. Nature Cell Biology, 2016, 18(1): 122-131.
[6] Wang H, Gau B, Slade W O, et al. The global phosphoproteome of Chlamydomonasreinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane. Molecular & Cellular Proteomics, 2014, 13(9): 2337-2353.
[7] Shi Y. Serine/threonine phosphatases: mechanism through structure. Cell, 2009, 139(3): 468-484.
[8] Grothe K, Hanke C, Momayezi M, et al. Functional characterization and localization of protein phosphatase type 2C from Paramecium. Journal of Biological Chemistry, 1998, 273(30): 19167-19172.
[9] Noguchi M, Sasaki J Y, Kamachi H, et al. Protein phosphatase 2C is involved in the cAMP‐dependent ciliary control in Paramecium caudatum. Cell Motility and the Cytoskeleton, 2003, 54(2): 95-104.
[10] Sager R, Granick S. Nutritional studies with Chlamydomonasreinhardi. Annals of the New York Academy of Sciences, 1953, 56(5): 831-838.
[11] Kim S, Tsiokas L. Cilia and cell cycle re-entry: more than a coincidence. Cell Cycle, 2011, 10(16): 2683-2690.
[12] Sung C H, Li A. Ciliary resorption modulates G1 length and cell cycle progression. Cell Cycle,2011, 10(17): 2825-2826.
[13] Hilton L K, Gunawardane K, Kim J W, et al. The kinases LF4 and CNK2 control ciliary length by feedback regulation of assembly and disassembly rates. Current Biology, 2013, 23(22): 2208-2214.
[14] Avidor-Reiss T, Gopalakrishnan J. Cell cycle regulation of the centrosome and cilium. Drug Discovery Today: Disease Mechanisms, 2013, 10(3): e119-e124.
[15] Parker J D K, Hilton L K, Diener D R, et al. Centrioles are freed from cilia by severing prior to mitosis. Cytoskeleton, 2010, 67(7): 425-430.
PDF(1187 KB)
/
| 〈 |
|
〉 |
