Channelrhodopsin-1: Cellular Localization and Role in Eyespot Assembly and Placement in Chlamydomonas reinhardtii

Persistent Link:
http://hdl.handle.net/10150/620817
Title:
Channelrhodopsin-1: Cellular Localization and Role in Eyespot Assembly and Placement in Chlamydomonas reinhardtii
Author:
Thompson, Mark David
Issue Date:
2016
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
The eyespot of the single-celled alga Chlamydomonas aids the cell in detecting the direction of light in the environment. The complex assembly and asymmetric placement of the eyespot provides a model to ask questions about assembly and asymmetric placement of organelles. Understanding the mechanisms that underlie assembly and asymmetric placement of the eyespot can be applied more broadly to their functions in other eukaryotic organisms. This study sought to understand the role of a key protein in those processes, Channelrhodopsin-1 (ChR1). ChR1 was found to localize along the entire length of the D4 rootlet from the region around the daughter basal body to the eyespot. ChR1 was found to primarily localize to the plasma membrane side of the D4, suggesting that ChR1 was being pulled through the plasma membrane from the region around the basal bodies to the eyespot. Further, ChR1 was found to be able to localize to the eyespot even with the truncation of the large cytoplasmic C-terminal domain, suggesting that ChR1 is able to complex with another protein that is being trafficked to the eyespot. One such protein was thought to be ChR2, the other light-activated ion channel localized to the eyespot. Efforts to isolate a mutation in ChR2 were unsuccessful. Initial efforts were made in this dissertation to perform proteomic studies of ChR1 and identify its interacting partners. ChR1 is not the master regulator of either placement or assembly of the eyespot, but work in this study lays the groundwork to further investigate transport of ChR1 and interacting proteins to the eyespot and their role in assembly of the eyespot.
Type:
text; Electronic Dissertation
Keywords:
ChR1; Eyespot; Molecular & Cellular Biology; Chlamydomonas
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Molecular & Cellular Biology
Degree Grantor:
University of Arizona
Advisor:
Dieckmann, Carol

Full metadata record

DC FieldValue Language
dc.language.isoen_USen
dc.titleChannelrhodopsin-1: Cellular Localization and Role in Eyespot Assembly and Placement in Chlamydomonas reinhardtiien_US
dc.creatorThompson, Mark Daviden
dc.contributor.authorThompson, Mark Daviden
dc.date.issued2016-
dc.publisherThe University of Arizona.en
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en
dc.description.abstractThe eyespot of the single-celled alga Chlamydomonas aids the cell in detecting the direction of light in the environment. The complex assembly and asymmetric placement of the eyespot provides a model to ask questions about assembly and asymmetric placement of organelles. Understanding the mechanisms that underlie assembly and asymmetric placement of the eyespot can be applied more broadly to their functions in other eukaryotic organisms. This study sought to understand the role of a key protein in those processes, Channelrhodopsin-1 (ChR1). ChR1 was found to localize along the entire length of the D4 rootlet from the region around the daughter basal body to the eyespot. ChR1 was found to primarily localize to the plasma membrane side of the D4, suggesting that ChR1 was being pulled through the plasma membrane from the region around the basal bodies to the eyespot. Further, ChR1 was found to be able to localize to the eyespot even with the truncation of the large cytoplasmic C-terminal domain, suggesting that ChR1 is able to complex with another protein that is being trafficked to the eyespot. One such protein was thought to be ChR2, the other light-activated ion channel localized to the eyespot. Efforts to isolate a mutation in ChR2 were unsuccessful. Initial efforts were made in this dissertation to perform proteomic studies of ChR1 and identify its interacting partners. ChR1 is not the master regulator of either placement or assembly of the eyespot, but work in this study lays the groundwork to further investigate transport of ChR1 and interacting proteins to the eyespot and their role in assembly of the eyespot.en
dc.typetexten
dc.typeElectronic Dissertationen
dc.subjectChR1en
dc.subjectEyespoten
dc.subjectMolecular & Cellular Biologyen
dc.subjectChlamydomonasen
thesis.degree.namePh.D.en
thesis.degree.leveldoctoralen
thesis.degree.disciplineGraduate Collegeen
thesis.degree.disciplineMolecular & Cellular Biologyen
thesis.degree.grantorUniversity of Arizonaen
dc.contributor.advisorDieckmann, Carolen
dc.contributor.committeememberCapaldi, Andrewen
dc.contributor.committeememberSchroeder, Joyceen
dc.contributor.committeememberWeinert, Teden
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