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Toward a model of the poliovirus rib...

Lyle, John Michael.

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Toward a model of the poliovirus ribonucleic acid replication complex.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Toward a model of the poliovirus ribonucleic acid replication complex./
作者:	Lyle, John Michael.
面頁冊數:	132 p.
附註:	Adviser: Karla Kirkegaard.
Contained By:	Dissertation Abstracts International63-04B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048575
ISBN:	0493629068

Toward a model of the poliovirus ribonucleic acid replication complex.
Lyle, John Michael.

Toward a model of the poliovirus ribonucleic acid replication complex. - 132 p.

Adviser: Karla Kirkegaard.

Thesis (Ph.D.)--Stanford University, 2002.

Poliovirus RNA replication occurs on the surface of virus-induced membranous vesicles. While the components of the RNA replication complex have been extensively studied, its structure on the surface of these membranes is still a matter of conjecture. It is the goal of this thesis to provide insight into the likely organization of this RNA replication complex. Biochemical, structural, and direct observation have been used to this end.

ISBN: 0493629068Subjects--Topical Terms:

1017734
Biology, Microbiology.

Toward a model of the poliovirus ribonucleic acid replication complex.
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245 1 0 $a Toward a model of the poliovirus ribonucleic acid replication complex.
300 $a 132 p.
500 $a Adviser: Karla Kirkegaard.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1683.
502 $a Thesis (Ph.D.)--Stanford University, 2002.
520 $a Poliovirus RNA replication occurs on the surface of virus-induced membranous vesicles. While the components of the RNA replication complex have been extensively studied, its structure on the surface of these membranes is still a matter of conjecture. It is the goal of this thesis to provide insight into the likely organization of this RNA replication complex. Biochemical, structural, and direct observation have been used to this end.
520 $a One section explores the interaction of viral proteins 3AB and 3B with the viral polymerase. 3AB anchors the polymerase to the surface of virus-induced vesicles. A detailed map of the interactions between 3AB and the polymerase demonstrates that 3AB binds to a discreet site on the polymerase. Residues involved in 3AB binding as well as nearby residues are vital for the addition of uridyl residues to 3B, the protein primer of RNA replication.
520 $a The following section characterizes the interaction of the poliovirus polymerase with other molecules of polymerase to form large, two-dimensional arrays in infected cells via interfaces observed in the crystal structure of the polymerase. The importance of these interactions in the replication of the viral genome is also considered, demonstrating that they are necessary for efficient RNA elongation, both for the catalytic function of nucleotide addition and for binding the substrate RNA in a manner that allows cooperative RNA replication. Further, it was found that the location of the 3AB and 3B interaction site predicts that these interactions should not interfere with the functioning of the polymerase as a high-order oligomer, suggesting that 3AB-polymerase and polymerase-polymerase interactions both function in the construction of the RNA replication complex. Evidence is also presented to suggest that these interactions occur in infected cells.
590 $a School code: 0212.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
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