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The role of F plasmid relaxosome pro...

Williams, Sarah L.

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The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation./
作者:	Williams, Sarah L.
面頁冊數:	255 p.
附註:	Adviser: Joel F. Schildbach.
Contained By:	Dissertation Abstracts International68-11B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3288554
ISBN:	9780549314011

The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation.
Williams, Sarah L.

The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation. - 255 p.

Adviser: Joel F. Schildbach.

Thesis (Ph.D.)--The Johns Hopkins University, 2008.

Bacterial conjugation is the transfer of single-stranded DNA (ssDNA) from one bacterium to another. The initiation of transfer requires a complex of proteins called the relaxosome. The F plasmid relaxosome includes plasmid-encoded proteins TraI and TraY along with host-encoded protein integration host factor (IHF). TraI consists of relaxase and helicase domain, which are responsible for nicking and unwinding ssDNA respectively at a site called nic located in the origin of transfer (oriT). TraY and IHF act as accessory proteins, which bind near nic and bend the DNA creating a ssDNA region suitable for TraI binding.

ISBN: 9780549314011Subjects--Topical Terms:

1017734
Biology, Microbiology.

The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation.
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100 1 $a Williams, Sarah L. $3 1263085
245 1 4 $a The role of F plasmid relaxosome protein binding sites and intervening origin of transfer (oriT) regions in bacterial conjugation.
300 $a 255 p.
500 $a Adviser: Joel F. Schildbach.
500 $a Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7330.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2008.
520 $a Bacterial conjugation is the transfer of single-stranded DNA (ssDNA) from one bacterium to another. The initiation of transfer requires a complex of proteins called the relaxosome. The F plasmid relaxosome includes plasmid-encoded proteins TraI and TraY along with host-encoded protein integration host factor (IHF). TraI consists of relaxase and helicase domain, which are responsible for nicking and unwinding ssDNA respectively at a site called nic located in the origin of transfer (oriT). TraY and IHF act as accessory proteins, which bind near nic and bend the DNA creating a ssDNA region suitable for TraI binding.
520 $a Both the TraI binding site, sbi, and the F-related relaxase TrwC binding site include an inverted repeat (IR). The TrwC relaxase domain recognizes this IR through a hairpin structure. Base substitutions within the sbi IR effect the initiation of transfer. However, previous TraI relaxase domain (TraI36) binding and structural experiments used an incomplete IR sequence. Therefore, Chapter 2 investigates the effects of base substitutions within the full IR on TraI36 binding and plasmid transfer. The IR within sbi is not essential for plasmid transfer, however the IR sequence does improve TraI36 binding and alters binding specificity.
520 $a Chapter 3 focuses on the relevance of TraY and IHF oriT binding sites and their spacing. Base substitutions created throughout both binding sites were assayed for binding affinity and mobilization efficiency. Half and full helical turns were inserted between the relaxosome protein binding sites and assayed for mobilization efficiency. Base substitutions showed a significant reduction in in vitro binding, but little effect on plasmid mobilization. In contrast, the insertions drastically reduced mobilization.
520 $a The TraY oriT binding site (sbyA) consists of three subsites. Two subsites are bound cooperatively with high affinity in an inverted fashion. The third TraY molecule binds with lower affinity in a similar orientation to its adjacent TraY molecule. TraY variants were generated and assessed for binding affinity and occupancy. The third TraY molecule interacts with its neighboring TraY molecule with a low level of cooperativity. TraY residues involved in the cooperative interfaces were elucidated and the overall orientation of all three TraY molecules was proposed.
590 $a School code: 0098.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0410
690 $a 0487
710 2 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 68-11B.
790 $a 0098
790 1 0 $a Schildbach, Joel F., $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3288554