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Roles of intraflagellar transport proteins and actins in cilia assembly and motility in Tetrahymena thermophila.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Roles of intraflagellar transport proteins and actins in cilia assembly and motility in Tetrahymena thermophila./
作者:	Tsao, Che-Chia.
面頁冊數:	1 online resource (209 pages)
附註:	Source: Dissertations Abstracts International, Volume: 68-07, Section: B.
Contained By:	Dissertations Abstracts International68-07B.
標題:	Cellular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3230325click for full text (PQDT)
ISBN:	9780542847295

Roles of intraflagellar transport proteins and actins in cilia assembly and motility in Tetrahymena thermophila.
Tsao, Che-Chia.

Roles of intraflagellar transport proteins and actins in cilia assembly and motility in Tetrahymena thermophila. - 1 online resource (209 pages)

Source: Dissertations Abstracts International, Volume: 68-07, Section: B.

Thesis (Ph.D.)--University of Rochester, 2006.

Includes bibliographical references

Cilia/flagella are conserved microtubule structures that generate motility or function as cell sensors. A subtractive hybridization screen was used to isolate genes induced during cilia regeneration. 91 genes were identified, which partially overlapped with genes identified by other genomic screens of cilia related genes. IFT172 and ACT2 were chosen for further of their roles in cilia assembly or motility. IFT122 and ACT1 were studied in parallel for comparison. IFT172 and IFT122 encode proteins involved in a bi-directional transport of materials along cilia but belong to two biochemically distinct complexes. IFT172, a complex B protein with an N-terminal WD and a C-terminal repeat domain, is required for cilia assembly. Neither of the two domains alone is sufficient to assemble cilia or localize to the cilia. Partial truncation of the C-terminal region does not abolish cilia assembly but causes accumulation of IFT proteins at ciliary tips, suggesting that the truncated C-terminal region of IFT172 is not required for anterograde transport but affects the anterograde/retrograde transition process or retrograde transport. IFT122, a complex A protein with a domain organization similar to IFT172, is not essential for cilia assembly or regeneration. Deletion of IFT122 causes other IFT proteins to preferentially accumulate at the ciliary tip, indicating that IFT122 is not required for anterograde transport but plays a role in returning the proteins from the ciliary tip to the cell body. Of the four actin genes are present in Tetrahymena genome, ACT2 is the only one induced during cilia regeneration. ACT1 is the principal actin gene expressed during vegetative growth. Neither ACT1 nor ACT2 is essential for viability or cilia biogenesis. ACT1 knockout cells lose ciliary motility and become paralyzed. ACT2 knockout cells possess motile cilia but swim more slowly. Only ACT1 but not the other 3 actins nor ACT1/ACT2 chimera can rescue the ACT1 knockout phenotype. Axoneme defects are observed in ACT1 knockout cells but not in the ACT2 knockout cells. Act1p could be detected in isolated cilia. Therefore ACT1 but not ACT2 plays a specific role in ciliary motility.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9780542847295Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

ActinsIndex Terms--Genre/Form:

542853
Electronic books.

Roles of intraflagellar transport proteins and actins in cilia assembly and motility in Tetrahymena thermophila.
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502 $a Thesis (Ph.D.)--University of Rochester, 2006.
504 $a Includes bibliographical references
520 $a Cilia/flagella are conserved microtubule structures that generate motility or function as cell sensors. A subtractive hybridization screen was used to isolate genes induced during cilia regeneration. 91 genes were identified, which partially overlapped with genes identified by other genomic screens of cilia related genes. IFT172 and ACT2 were chosen for further of their roles in cilia assembly or motility. IFT122 and ACT1 were studied in parallel for comparison. IFT172 and IFT122 encode proteins involved in a bi-directional transport of materials along cilia but belong to two biochemically distinct complexes. IFT172, a complex B protein with an N-terminal WD and a C-terminal repeat domain, is required for cilia assembly. Neither of the two domains alone is sufficient to assemble cilia or localize to the cilia. Partial truncation of the C-terminal region does not abolish cilia assembly but causes accumulation of IFT proteins at ciliary tips, suggesting that the truncated C-terminal region of IFT172 is not required for anterograde transport but affects the anterograde/retrograde transition process or retrograde transport. IFT122, a complex A protein with a domain organization similar to IFT172, is not essential for cilia assembly or regeneration. Deletion of IFT122 causes other IFT proteins to preferentially accumulate at the ciliary tip, indicating that IFT122 is not required for anterograde transport but plays a role in returning the proteins from the ciliary tip to the cell body. Of the four actin genes are present in Tetrahymena genome, ACT2 is the only one induced during cilia regeneration. ACT1 is the principal actin gene expressed during vegetative growth. Neither ACT1 nor ACT2 is essential for viability or cilia biogenesis. ACT1 knockout cells lose ciliary motility and become paralyzed. ACT2 knockout cells possess motile cilia but swim more slowly. Only ACT1 but not the other 3 actins nor ACT1/ACT2 chimera can rescue the ACT1 knockout phenotype. Axoneme defects are observed in ACT1 knockout cells but not in the ACT2 knockout cells. Act1p could be detected in isolated cilia. Therefore ACT1 but not ACT2 plays a specific role in ciliary motility.
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650 4 $a Molecular biology. $3 517296
650 4 $a Genetics. $3 530508
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653 $a Actins
653 $a Cilia
653 $a Intraflagellar transport
653 $a Motility
653 $a Tetrahymena thermophila
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773 0 $t Dissertations Abstracts International $g 68-07B.
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