Architectural investigation of the intraflagellar transport complex B of Chlamydomonas reinhardtii


Lucker, Ben F.Jr.. (2007). Architectural investigation of the intraflagellar transport complex B of Chlamydomonas reinhardtii. Theses and Dissertations Collection, University of Idaho Library Digital Collections.

Architectural investigation of the intraflagellar transport complex B of Chlamydomonas reinhardtii
Lucker, Ben F.Jr.
Chlamydomonas reinhardtii Microorganisms--Motility Flagella (Microbiology)
Microbiology, Molecular Biology, and Biochemistry
The terms cilia and flagella are synonymous terms for a membrane bounded organelles, which extend 3-30 [mu]m into the extracellular environment. Many cilia such those found on sperm provide a mechanism for cellular motility. Others, like tracheal epithelial cilia, are used for bulk fluid movement. Many non-motile cilia, such as those found in olfactory tissues, are used primarily for signal transduction. Indeed, throughout the human body, many cells have a primary cilium which monitors the local environment. Defects in this sensory organelle have been tied to a growing list of human diseases, termed ciliopathies. Some of these include polycystic kidney disease, ocular degeneration, primary cilia dyskinesia, situs inversus, and both male and female infertility. Understanding the assembly and function of these organelles will be an important step toward understanding the mechanism of these diseases. Intraflagellar transport or IFT is a universal process required for proper ciliary function and assembly within eukaryotes. IFT is characterized by the movement of large proteinaceous complexes, termed IFT particles, from the cell body to the flagellar tip (anterograde IFT) and back to the cell body (retrograde IFT). To study the IFT process we use the biflagellate unicellular green alga, Chlamydomonas reinhardtii. Chlamydomonas was the model organism in which IFT was first identified, and remains the only organism from which native IFT proteins have been isolated. Each IFT particle contains multiple copies of two large structural complexes called A and B. Complex A contains at least six proteins ranging in size from 144-43 kDa, whereas complex B contains at least 13 proteins ranging in size from 172-20 kDa. The primary focus of this dissertation was to lay the foundation for understanding the architecture of the IFT complex B. Here we report that complex B contains a core of salt-stable proteins consisting of IFT88, IFT81, IFT74/72, IFT52, IFT46, IFT27, IFT25, and IFT22. Of the core subunits, IFT81 and IFT74/72 can form a heterotetrameric sub-complex, while IFT88, IFT52, and IFT46 can form a separate ternary sub-complex. Additionally we identified the presence of a "supra" IFT complex in gametic cells and a novel localization of the anterograde IFT motor kinesin-2 before and during the mating of Chlamydomonas.
Thesis (Ph. D., Microbiology, Molecular Biology, and Biochemistry)--University of Idaho, January 2007.
Major Professor:
Douglas G. Cole.
Defense Date:
January 2007.
Format Original:
xi, 120 leaves :ill. (some col.) ;29 cm.

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