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Single-Molecule Study of Neuronal t-...

Znahg, Xinming.

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Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers./
Author:	Znahg, Xinming.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2016,
Description:	89 p.
Notes:	Source: Dissertation Abstracts International, Volume: 78-01(E), Section: B.
Contained By:	Dissertation Abstracts International78-01B(E).
Subject:	Biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10160839
ISBN:	9781369157345

Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers.
Znahg, Xinming.

Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers. - Ann Arbor : ProQuest Dissertations & Theses, 2016 - 89 p.

Source: Dissertation Abstracts International, Volume: 78-01(E), Section: B.

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

Soluble N-ethylmaleimide-sensitive factor attachment proteins (SNAREs) couple their stepwise folding to membrane fusion. For numerous SNAREs, the first and rate-limiting step of their folding is the assembly of t-SNAREs into a binary complex. However, the structure, stability, and dynamics of this t-SNARE complex remain elusive. Here we show that the neuronal t-SNARE complex is a three-helix bundle with a frayed C-terminus using a single-molecule manipulation approach based on high-resolution optical tweezers. The helical bundle contains two sequentially folding domains: an N-terminal domain (NTD) and a C-terminal domain (CTD). A central ionic layer separates the two domains and plays a critical role in t-SNARE folding. Point mutation of the ionic layer alters the folding pathway and structure of the t-SNARE complex. The folding of the wild-type t-SNARE complex releases a total free energy of ~10.5 kBT, with ~4.8 kBT in the NTD and ~5.7 kBT in the CTD. The binding of v-SNARE VAMP-2 to the NTD of the t-SNARE complex stabilizes the CTD of the complex, thereby facilitating rapid zippering at the CTD during membrane fusion. Our results support the SNARE zippering model and provide a molecular mechanism for the hypothesis that t-SNAREs act as a zippering template for v-SNARE during membrane fusion.

ISBN: 9781369157345Subjects--Topical Terms:

522710
Biology.

Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers.
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245 1 0 $a Single-Molecule Study of Neuronal t-SNARE Structure, Stability and Dynamics Using Optical Tweezers.
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300 $a 89 p.
500 $a Source: Dissertation Abstracts International, Volume: 78-01(E), Section: B.
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502 $a Thesis (Ph.D.)--Yale University, 2016.
520 $a Soluble N-ethylmaleimide-sensitive factor attachment proteins (SNAREs) couple their stepwise folding to membrane fusion. For numerous SNAREs, the first and rate-limiting step of their folding is the assembly of t-SNAREs into a binary complex. However, the structure, stability, and dynamics of this t-SNARE complex remain elusive. Here we show that the neuronal t-SNARE complex is a three-helix bundle with a frayed C-terminus using a single-molecule manipulation approach based on high-resolution optical tweezers. The helical bundle contains two sequentially folding domains: an N-terminal domain (NTD) and a C-terminal domain (CTD). A central ionic layer separates the two domains and plays a critical role in t-SNARE folding. Point mutation of the ionic layer alters the folding pathway and structure of the t-SNARE complex. The folding of the wild-type t-SNARE complex releases a total free energy of ~10.5 kBT, with ~4.8 kBT in the NTD and ~5.7 kBT in the CTD. The binding of v-SNARE VAMP-2 to the NTD of the t-SNARE complex stabilizes the CTD of the complex, thereby facilitating rapid zippering at the CTD during membrane fusion. Our results support the SNARE zippering model and provide a molecular mechanism for the hypothesis that t-SNAREs act as a zippering template for v-SNARE during membrane fusion.
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