Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila
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ndltd-OhioLink-oai-etd.ohiolink.edu-miami12719772272021-08-03T05:40:48Z Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila KABI, AMRITA Cellular Biology cilia axoneme dynein hydin hydrocephalus Tetrahymena thermophila LC-MS/MS The focuses of my doctoral research were: (a) Dynein family of motors and (b) Hydrocephalus inducing protein – Hydin. Axonemal dyneins are molecular motors composed of heavy chains (HCs), intermediate and light chains. HCs comprise of the motor domain and make up most of the mass of the dynein complex. Previous studies identified eight inner arm dynein HC (DHC) in different ciliated and flagellated organisms. Recent comparative sequence analyses using completed genomes of different species resulted in identification of additional one-headed dynein HC genes in most of the organisms examined. Our proteomic studies using Tetrahymena axonemes revealed that most, if not all the dyneins are present in the axoneme and they are present in varying abundances. Functional studies with some dyneins knockouts generated suggest that dyneins are not completely redundant. Initial evidences suggest that there might be some compensation effect of other inner arm dyneins when one inner arm dynein is lost. Congenital hydrocephalus, a common birth defect, is characterized by the over accumulation of cerebrospinal fluid (CSF) within the ventricular system of the brain. Mutations in hydin result in hydrocephalus in hy3 homozygous mice. Hydin was localized to ependymal cells in the brain, but it was not known whether mutations in hydin cause hydrocephalus by impairing ciliary motility leading to disruption of CSF fluid flow, or by some other mechanisms such as signaling defects. Comparative genomics identified homologs of the hydin gene in small organisms possessing motile cilia and flagella. To determine whether hydin causes hydrocephalus by impairing ciliary motility, I knocked out hydin gene in Tetrahymena. Mutating hydin gene had a dramatic effect on cell motility. Electron microscopic studies of axonemes isolated from mutant cells showed that lack a partial central pair indicating that it is a central pair protein (Kabi et al., In prep). Hence, these results show that hydin in essential for normal ciliary motility. Ciliary movement is essential for normal CSF flow and thus, mutations in hydin can cause hydrocephalus by impairing ciliary motility. 2010-04-23 English text Miami University / OhioLINK http://rave.ohiolink.edu/etdc/view?acc_num=miami1271977227 http://rave.ohiolink.edu/etdc/view?acc_num=miami1271977227 unrestricted This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws. |
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language |
English |
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topic |
Cellular Biology cilia axoneme dynein hydin hydrocephalus Tetrahymena thermophila LC-MS/MS |
spellingShingle |
Cellular Biology cilia axoneme dynein hydin hydrocephalus Tetrahymena thermophila LC-MS/MS KABI, AMRITA Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
author |
KABI, AMRITA |
author_facet |
KABI, AMRITA |
author_sort |
KABI, AMRITA |
title |
Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
title_short |
Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
title_full |
Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
title_fullStr |
Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
title_full_unstemmed |
Role of Inner Arm Dyneins and Hydin in Ciliary Motility in Tetrahymena thermophila |
title_sort |
role of inner arm dyneins and hydin in ciliary motility in tetrahymena thermophila |
publisher |
Miami University / OhioLINK |
publishDate |
2010 |
url |
http://rave.ohiolink.edu/etdc/view?acc_num=miami1271977227 |
work_keys_str_mv |
AT kabiamrita roleofinnerarmdyneinsandhydininciliarymotilityintetrahymenathermophila |
_version_ |
1719423522940387328 |