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

Single-molecule studies of metal hom...

Santiago, Ace George Guanez.

FindBook

Google Book

Amazon

博客來

Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells./
作者:	Santiago, Ace George Guanez.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2016,
面頁冊數:	219 p.
附註:	Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.
Contained By:	Dissertation Abstracts International78-02B(E).
標題:	Chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10171447
ISBN:	9781369254846

Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells.
Santiago, Ace George Guanez.

Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells. - Ann Arbor : ProQuest Dissertations & Theses, 2016 - 219 p.

Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.

Thesis (Ph.D.)--Cornell University, 2016.

This item is not available from ProQuest Dissertations & Theses.

This thesis dissertation has two chapters: Chapter I is a published research, and Chapter II is a research in progress.

ISBN: 9781369254846Subjects--Topical Terms:

516420
Chemistry.

Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells.
LDR:03589nmm a2200337 4500 001 2124002
005 20171023101704.5
008 180830s2016 ||||||||||||||||| ||eng d
020 $a 9781369254846
035 $a (MiAaPQ)AAI10171447
035 $a AAI10171447
040 $a MiAaPQ $c MiAaPQ
100 1 $a Santiago, Ace George Guanez. $3 3285963
245 1 0 $a Single-molecule studies of metal homeostasis dynamics by CueR, ZntR, and CusCBA complex in live Escherichia coli cells.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2016
300 $a 219 p.
500 $a Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.
500 $a Adviser: Peng Chen.
502 $a Thesis (Ph.D.)--Cornell University, 2016.
506 $a This item is not available from ProQuest Dissertations & Theses.
520 $a This thesis dissertation has two chapters: Chapter I is a published research, and Chapter II is a research in progress.
520 $a Chapter I. Binding and unbinding of transcription regulators at operator sites constitute a primary mechanism for gene regulation. While many cellular factors are known to regulate their binding, little is known on how cells can modulate their unbinding for regulation. Using nanometer-precision singlemolecule tracking, we study the unbinding kinetics from DNA of two metal-sensing transcription regulators in living Escherichia coli cells. We find that they show unusual concentration-dependent unbinding kinetics from chromosomal recognition sites in both their apo- and holo-forms. Unexpectedly, their unbinding kinetics further vary with the extent of chromosome condensation, and more surprisingly, vary in opposite ways for their apo-repressor vs. holo-activator forms. These findings suggest novel and likely broadly relevant mechanisms for facile switching between transcription activation and deactivation in vivo and in coordinating transcription regulation of resistance genes with the cell cycle.
520 $a Chapter II. Tripartite resistance-nodulation-division (RND) family of efflux pumps serve as major efflux systems in Gram-negative bacteria for expelling diverse toxic compounds, including clinically relevant antibiotics, from their cytosol and/or periplasm to the extracellular space. The mechanism of how tripartite efflux pumps operate without compromising the dynamic nature of the periplasm remains unknown. Using nanometer-precision single-molecule tracking, we study the population of the different diffusion states of CusA, an inner membrane protein and a component of the CusCBA complex in E. coli, which is an RND-type of efflux pump. We find that the slow state of CusA, a state corresponding to the fully assembled CusCBA complex, increases in the presence of copper in the environment, and only does so if both CusC and CusB are present. In addition, the intracellular concentration of CusA does not increase in the presence of copper even though mRNA levels of CusA, CusB, and CusC increase, suggesting that in order to effectively efflux copper from the cytosol, the cell resorts to assembling more of the CusCBA complex, rather than expressing more of the CusA protein. Taken together, our data are consistent with the assembly-disassembly model for copper efflux by the CusCBA complex, which could be a broadly relevant mechanism to other RND-type of efflux pumps.
590 $a School code: 0058.
650 4 $a Chemistry. $3 516420
650 4 $a Biophysics. $3 518360
650 4 $a Biochemistry. $3 518028
690 $a 0485
690 $a 0786
690 $a 0487
710 2 $a Cornell University. $3 530586
773 0 $t Dissertation Abstracts International $g 78-02B(E).
790 $a 0058
791 $a Ph.D.
792 $a 2016
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10171447