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Trypanin is a novel microtubule-asso...

Hutchings, Nathan Robert.

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Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei./
Author:	Hutchings, Nathan Robert.
Description:	182 p.
Notes:	Source: Dissertation Abstracts International, Volume: 62-07, Section: B, page: 3033.
Contained By:	Dissertation Abstracts International62-07B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3018582
ISBN:	0493299785

Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei.
Hutchings, Nathan Robert.

Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei. - 182 p.

Source: Dissertation Abstracts International, Volume: 62-07, Section: B, page: 3033.

Thesis (Ph.D.)--The University of Iowa, 2001.

Although there has been extensive ultrastructural analysis of the trypanosome cytoskeleton, understanding of the molecular composition of the trypanosome cytoskeleton is still rudimentary. Several trypanosome proteins are targeted to the flagellar pocket; the sole site of secretion in trypanosomes. However, the signals responsible for flagellar pocket targeting are currently unknown. Trypanin is a 54-kDa protein from Trypanosoma brucei that was thought to be released from trypanosomes. Using trypanin-green fluorescent protein (trypanin-GFP) fusion proteins, an internal 144 amino acid domain was shown to direct GFP to the cytoplasmic side of the flagellar pocket via a structural motif. Immuno-electron microscopy shows that the trypanin-GFP protein localizes to an electron dense structure that abuts the flagellar pocket membrane, a localization that can be disrupted by point mutations within the targeting-domain. The localization of targeting domain mutants and a human-trypanin GFP fusion protein suggest that flagellar pocket targeting involves interactions with the trypanosome cytoskeleton.

ISBN: 0493299785Subjects--Topical Terms:

1017686
Biology, Cell.

Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei.
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100 1 $a Hutchings, Nathan Robert. $3 1952613
245 1 0 $a Trypanin is a novel microtubule-associated protein in the African trypanosome, Trypanosoma brucei.
300 $a 182 p.
500 $a Source: Dissertation Abstracts International, Volume: 62-07, Section: B, page: 3033.
500 $a Supervisor: John E. Donelson.
502 $a Thesis (Ph.D.)--The University of Iowa, 2001.
520 $a Although there has been extensive ultrastructural analysis of the trypanosome cytoskeleton, understanding of the molecular composition of the trypanosome cytoskeleton is still rudimentary. Several trypanosome proteins are targeted to the flagellar pocket; the sole site of secretion in trypanosomes. However, the signals responsible for flagellar pocket targeting are currently unknown. Trypanin is a 54-kDa protein from Trypanosoma brucei that was thought to be released from trypanosomes. Using trypanin-green fluorescent protein (trypanin-GFP) fusion proteins, an internal 144 amino acid domain was shown to direct GFP to the cytoplasmic side of the flagellar pocket via a structural motif. Immuno-electron microscopy shows that the trypanin-GFP protein localizes to an electron dense structure that abuts the flagellar pocket membrane, a localization that can be disrupted by point mutations within the targeting-domain. The localization of targeting domain mutants and a human-trypanin GFP fusion protein suggest that flagellar pocket targeting involves interactions with the trypanosome cytoskeleton.
520 $a Little is known about the non-tubulin cytoskeleton-associated proteins in trypanosomes. Using biochemical fractionation, trypanin was shown to associate with the detergent-resistant and Ca++-resistant fraction of the trypanosome cytoskeleton, which contains several cytoskeletal complexes that function in cell motility, cytokinesis, and organelle inheritance. Trypanin-related genes are present in various eukaryotic organisms, and a human growth-arrest-specific protein (Gas11) that is 60% similar in sequence to trypanin, contains a domain that directs GFP to microtubules in mammalian cells. This suggests that trypanin represents a new protein family, whose members contribute to cytoskeleton function in species as diverse as protozoa and mammals.
520 $a In African trypanosomes, trypanin immunolocalizes along the trypanosome flagellum, and cells depleted of trypanin by double-stranded RNA interference (dsRNAi) have been shown to have a dramatic motility defect. Cytoskeletons isolated from trypanin-depleted cells have flagellar attachment defects, and electron microscopy reveals that trypanin stabilizes the attachment between the flagellum and the subpellicular cytoskeleton. Thus, trypanin is a cytoskeletal protein that associates with and localizes to the trypanosome flagellum where it is involved in conjoining cytoskeletal structures that attach the flagellum to the cell body.
590 $a School code: 0096.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
690 $a 0379
690 $a 0369
690 $a 0307
710 2 0 $a The University of Iowa. $3 1017439
773 0 $t Dissertation Abstracts International $g 62-07B.
790 1 0 $a Donelson, John E., $e advisor
790 $a 0096
791 $a Ph.D.
792 $a 2001
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3018582