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Regulation of myosin II bipolar thic...

Hostetter, Daniel.

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Regulation of myosin II bipolar thick filament assembly.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Regulation of myosin II bipolar thick filament assembly./
作者:	Hostetter, Daniel.
面頁冊數:	225 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5308.
Contained By:	Dissertation Abstracts International64-11B.
標題:	Biology, Cell. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3111729

Regulation of myosin II bipolar thick filament assembly.
Hostetter, Daniel.

Regulation of myosin II bipolar thick filament assembly. - 225 p.

Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5308.

Thesis (Ph.D.)--Stanford University, 2004.

Thick filament formation in Dictyostelium is an attractive candidate for deciphering determinants of self-assembly as all the information required to form a structure of defined size is contained in the myosin molecule itself. In addition, the assembly state of this complex can be dramatically changed by phosphorylation of only three threonine residues. We characterized bacterially expressed fragments of the coiled-coil tail to define what portion of the myosin molecule is required for regulated self-assembly. Tail fragments form paracrystals, structures that are highly organized but contain an undefined number of elements. While tail fragments do not form bipolar thick filaments, they have similar solubility properties to full-length myosin.Subjects--Topical Terms:

1017686
Biology, Cell.

Regulation of myosin II bipolar thick filament assembly.
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245 1 0 $a Regulation of myosin II bipolar thick filament assembly.
300 $a 225 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5308.
500 $a Adviser: James A. Spudich.
502 $a Thesis (Ph.D.)--Stanford University, 2004.
520 $a Thick filament formation in Dictyostelium is an attractive candidate for deciphering determinants of self-assembly as all the information required to form a structure of defined size is contained in the myosin molecule itself. In addition, the assembly state of this complex can be dramatically changed by phosphorylation of only three threonine residues. We characterized bacterially expressed fragments of the coiled-coil tail to define what portion of the myosin molecule is required for regulated self-assembly. Tail fragments form paracrystals, structures that are highly organized but contain an undefined number of elements. While tail fragments do not form bipolar thick filaments, they have similar solubility properties to full-length myosin.
520 $a Determination of the solubility of a series of tail fragments identified the C-terminal 68 kD of the tail as the minimal domain for regulated assembly (termed A.D. to C-terminus tail fragment). The charged amino acids in the A.D. to C-terminus tail fragment are organized into repeating blocks of 28 and 196 amino acids. Our analysis suggests that these charge repeats must be delicately balanced for efficient self-assembly and that the introduction of negative charge by phosphorylation is sufficient to regulate assembly.
520 $a GFP was fused to the N-terminus of the A.D. to C-terminus tail fragment to determine if a globular head is sufficient to limit the size of a thick filament. The GFP A.D. to C-terminus tail fragment undergoes regulated assembly into bipolar thick filaments that are structurally homologous to thick filaments formed from full-length myosin. The symmetrical distribution of both the 28 amino acid and 196 amino acid charge repeats in the A.D. to C-terminus tail fragment enabled us to test whether thick filament assembly requires specific amino acid sequences proximal to the globular head or an overall charge pattern. The A.D. to C-terminus tail fragment with GFP fused to the C-terminus undergoes regulated assembly into bipolar thick filaments, suggesting that assembly is driven by an overall charge pattern. In summary, we have reduced regulated assembly to a smaller and more manageable model system that promises to be a useful reagent in defining the determinants of myosin self-assembly.
590 $a School code: 0212.
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791 $a Ph.D.
792 $a 2004
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