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Characterizing the RNA-binding and c...

Brescia, Cristin Coco.

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Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq./
Author:	Brescia, Cristin Coco.
Description:	175 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 5912.
Contained By:	Dissertation Abstracts International64-12B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3117017

Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq.
Brescia, Cristin Coco.

Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq. - 175 p.

Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 5912.

Thesis (Ph.D.)--Medical College of Ohio at Toledo, 2003.

The DsrA RNA in E. coli controls the translation of two global regulatory proteins, RpoS and H-NS. DsrA activates the translation of rpoS while repressing the translation of H-NS. The protein Hfq is necessary for DsrA to function in vivo. Although Hfq binds to DsrA in vitro, the effect of Hfq on the structure of DsrA is not known. We have examined the structure of DsrA bound to Hfq in vitro by comparison of free DsrA in the presence and absence of Hfq using RNase footprinting, circular dichroism and thermal melt profiles. We demonstrate that Hfq does not alter the secondary structure of DsrA, but may affect its tertiary conformation. In addition, we identify the Hfq binding-site on DsrA and also demonstrate that binding occurs in the AAJ rich domain of DsrA.Subjects--Topical Terms:

1017734
Biology, Microbiology.

Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq.
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035 $a (UnM)AAI3117017
035 $a AAI3117017
040 $a UnM $c UnM
100 1 $a Brescia, Cristin Coco. $3 1948679
245 1 0 $a Characterizing the RNA-binding and chaperone activities of the Escherichia coli proteins, H-NS and Hfq.
300 $a 175 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 5912.
500 $a Adviser: Darren D. Sledjeski.
502 $a Thesis (Ph.D.)--Medical College of Ohio at Toledo, 2003.
520 $a The DsrA RNA in E. coli controls the translation of two global regulatory proteins, RpoS and H-NS. DsrA activates the translation of rpoS while repressing the translation of H-NS. The protein Hfq is necessary for DsrA to function in vivo. Although Hfq binds to DsrA in vitro, the effect of Hfq on the structure of DsrA is not known. We have examined the structure of DsrA bound to Hfq in vitro by comparison of free DsrA in the presence and absence of Hfq using RNase footprinting, circular dichroism and thermal melt profiles. We demonstrate that Hfq does not alter the secondary structure of DsrA, but may affect its tertiary conformation. In addition, we identify the Hfq binding-site on DsrA and also demonstrate that binding occurs in the AAJ rich domain of DsrA.
520 $a Although H-NS represses the transcription of over 100 genes, evidence suggests that H-NS can also affect the translation of some genes. One notable translational target of H-NS is the sigma factor rpoS. We examined the ability of H-NS to bind to the rpoS mRNA and one of its non-coding RNA regulators, DsrA, in vitro. We found that the apparent KD of our purified H-NS preparation binding to rpoS mRNA or DsrA RNA is near that of its preferred substrate curved DNA. In ribonuclease probing of H-NS:RNA complexes, we observe enhancement of RNA cleavage. Furthermore, this effect was also observed in vivo, leading us to propose that H-NS alters the tertiary structure of RNAs.
590 $a School code: 0539.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0410
690 $a 0307
690 $a 0487
710 2 0 $a Medical College of Ohio at Toledo. $3 1262748
773 0 $t Dissertation Abstracts International $g 64-12B.
790 1 0 $a Sledjeski, Darren D., $e advisor
790 $a 0539
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3117017