東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Intranuclear localization of the her...

Taylor, Travis J.

FindBook

Google Book

Amazon

博客來

Intranuclear localization of the herpes simplex virus ICP8 protein.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Intranuclear localization of the herpes simplex virus ICP8 protein./
作者:	Taylor, Travis J.
面頁冊數:	253 p.
附註:	Adviser: David M. Knipe.
Contained By:	Dissertation Abstracts International63-04B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051302
ISBN:	0493659234

Intranuclear localization of the herpes simplex virus ICP8 protein.
Taylor, Travis J.

Intranuclear localization of the herpes simplex virus ICP8 protein. - 253 p.

Adviser: David M. Knipe.

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

Herpes simplex virus (HSV) replication is regulated spatially within the nucleus of an infected cell. Viral processes such as DNA synthesis, transcription, capsid assembly, and DNA packaging all occur within specialized intranuclear structures called replication compartments. The HSV single-stranded DNA-binding protein, ICP8, localizes to these structures and is required for their formation. In this thesis, I addressed the questions of where and how do HSV replication compartments develop in the nucleus of an infected cell using an ICP8-GFP fusion protein as a model protein. Replication compartments are hypothesized to mature from a few distinct structures, called prereplicative sites, that form adjacent to cellular nuclear-matrix associated ND10 sites. Using the intranuclear localization of the HSV-1 single-stranded DNA-binding protein ICP8 fused to green fluorescent protein as a marker for replication compartments, I show in these studies that replication compartments started at a few punctate structures early in infection. Large replication compartments formed when small structures either moved through the intranuclear space to coalesce with adjacent compartments or increased in size by accretion and fused with neighboring structures. I further demonstrated that a proteasome-dependent protein degradation event was required for replication compartment maturation as the addition of the proteasome inhibitor, MG132, blocked compartment development. Also in this thesis, I used site-specific and random mutagenesis techniques to identify residues within the C-terminus of ICP8 that are required for intranuclear localization to prereplicative sites. Proline substitutions in a predicted C-terminal alpha-helix generated an ICP8 molecule that did not localize properly within the nucleus and acted in a dominant-negative manner. I proposed that ICP8 requires a C-terminal alpha-helix for intranuclear localization, possibly for binding cellular or viral factors required to target or retain ICP8 at specific intranuclear sites.

ISBN: 0493659234Subjects--Topical Terms:

1017734
Biology, Microbiology.

Intranuclear localization of the herpes simplex virus ICP8 protein.
LDR:02911nam 2200277 a 45 001 927776
005 20110425
008 110425s2002 eng d
020 $a 0493659234
035 $a (UnM)AAI3051302
035 $a AAI3051302
040 $a UnM $c UnM
100 1 $a Taylor, Travis J. $3 1251339
245 1 0 $a Intranuclear localization of the herpes simplex virus ICP8 protein.
300 $a 253 p.
500 $a Adviser: David M. Knipe.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1713.
502 $a Thesis (Ph.D.)--Harvard University, 2002.
520 $a Herpes simplex virus (HSV) replication is regulated spatially within the nucleus of an infected cell. Viral processes such as DNA synthesis, transcription, capsid assembly, and DNA packaging all occur within specialized intranuclear structures called replication compartments. The HSV single-stranded DNA-binding protein, ICP8, localizes to these structures and is required for their formation. In this thesis, I addressed the questions of where and how do HSV replication compartments develop in the nucleus of an infected cell using an ICP8-GFP fusion protein as a model protein. Replication compartments are hypothesized to mature from a few distinct structures, called prereplicative sites, that form adjacent to cellular nuclear-matrix associated ND10 sites. Using the intranuclear localization of the HSV-1 single-stranded DNA-binding protein ICP8 fused to green fluorescent protein as a marker for replication compartments, I show in these studies that replication compartments started at a few punctate structures early in infection. Large replication compartments formed when small structures either moved through the intranuclear space to coalesce with adjacent compartments or increased in size by accretion and fused with neighboring structures. I further demonstrated that a proteasome-dependent protein degradation event was required for replication compartment maturation as the addition of the proteasome inhibitor, MG132, blocked compartment development. Also in this thesis, I used site-specific and random mutagenesis techniques to identify residues within the C-terminus of ICP8 that are required for intranuclear localization to prereplicative sites. Proline substitutions in a predicted C-terminal alpha-helix generated an ICP8 molecule that did not localize properly within the nucleus and acted in a dominant-negative manner. I proposed that ICP8 requires a C-terminal alpha-helix for intranuclear localization, possibly for binding cellular or viral factors required to target or retain ICP8 at specific intranuclear sites.
590 $a School code: 0084.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0410
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0084
790 1 0 $a Knipe, David M., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051302