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Molecular Mechanism of Secretory Pro...

Bauer, Benedikt Werner.

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Molecular Mechanism of Secretory Protein Translocation by the SecA-ATPase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Molecular Mechanism of Secretory Protein Translocation by the SecA-ATPase./
作者:	Bauer, Benedikt Werner.
面頁冊數:	173 p.
附註:	Source: Dissertation Abstracts International, Volume: 77-04(E), Section: B.
Contained By:	Dissertation Abstracts International77-04B(E).
標題:	Cellular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3738693
ISBN:	9781339291727

Molecular Mechanism of Secretory Protein Translocation by the SecA-ATPase.
Bauer, Benedikt Werner.

Molecular Mechanism of Secretory Protein Translocation by the SecA-ATPase. - 173 p.

Source: Dissertation Abstracts International, Volume: 77-04(E), Section: B.

Thesis (Ph.D.)--Harvard University, 2015.

In bacteria, most secretory proteins are translocated across the plasma membrane by the interplay of the SecA ATPase and the SecY channel. How SecA moves a broad range of polypeptide substrates is only poorly understood. Here, we use a combination of bulk biochemistry and single molecule Foerster Resonance Energy Transfer (smFRET) assays to show that SecA moves polypeptides through the SecY-channel by a "push and slide" mechanism. In its ATP-bound state, SecA interacts through a two- helix finger with a subset of amino acids in a substrate, pushing them into the channel. A polypeptide can also passively slide back and forth when SecA is in the predominant ADP-bound state, or when SecA encounters a poorly interacting amino acid in its ATP- bound state. SecA performs multiple rounds of ATP hydrolysis before dissociating from SecY. The proposed "push and slide" mechanism is supported by a mathematical model and explains how SecA moves polypeptides independently of their sequence. This mechanism may also apply to hexameric polypeptide-translocating ATPases.

ISBN: 9781339291727Subjects--Topical Terms:

3172791
Cellular biology.

Molecular Mechanism of Secretory Protein Translocation by the SecA-ATPase.
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502 $a Thesis (Ph.D.)--Harvard University, 2015.
520 $a In bacteria, most secretory proteins are translocated across the plasma membrane by the interplay of the SecA ATPase and the SecY channel. How SecA moves a broad range of polypeptide substrates is only poorly understood. Here, we use a combination of bulk biochemistry and single molecule Foerster Resonance Energy Transfer (smFRET) assays to show that SecA moves polypeptides through the SecY-channel by a "push and slide" mechanism. In its ATP-bound state, SecA interacts through a two- helix finger with a subset of amino acids in a substrate, pushing them into the channel. A polypeptide can also passively slide back and forth when SecA is in the predominant ADP-bound state, or when SecA encounters a poorly interacting amino acid in its ATP- bound state. SecA performs multiple rounds of ATP hydrolysis before dissociating from SecY. The proposed "push and slide" mechanism is supported by a mathematical model and explains how SecA moves polypeptides independently of their sequence. This mechanism may also apply to hexameric polypeptide-translocating ATPases.
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