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Chaperone function of the botulinum ...

University of California, San Diego., Biology.

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Chaperone function of the botulinum neurotoxin protein translocating channel.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Chaperone function of the botulinum neurotoxin protein translocating channel./
Author:	Fischer, Audrey.
Description:	190 p.
Notes:	Adviser: Mauricio Montal.
Contained By:	Dissertation Abstracts International68-11B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3289445
ISBN:	9780549337188

Chaperone function of the botulinum neurotoxin protein translocating channel.
Fischer, Audrey.

Chaperone function of the botulinum neurotoxin protein translocating channel. - 190 p.

Adviser: Mauricio Montal.

Thesis (Ph.D.)--University of California, San Diego, 2008.

Clostridial botulinum neurotoxins (BoNTs) induce neuroparalysis by arresting synaptic exocytosis. BoNT consists of three functional domains: protease, translocation and receptor binding, and is cleaved into two disulfide linked, polypeptide chains: Light chain (LC) protease and Heavy chain (HC) translocon and receptor binding. One of the most elusive and intriguing steps of the BoNT intoxication process is the translocation of the proteolytic LC through the BoNT protein-conducting channel of the HC, from the endosomal compartment to the cytosol. In this dissertation, we utilize single-particle electron microscopy to resolve the discrepancies in multi-domain arrangement between different isoforms of BoNT in an effort to visualize rearrangement of domains and conformational changes associated with the translocation process. We investigate the dynamics of protein-translocation focusing on the interactions between the HC channel/chaperone and its LC cargo. Single molecule translocation was monitored in real time using excised patches of neuronal cells. LC translocation requires translocation domain (TD) insertion in a receptor binding domain (RBD) dependent manner, coupled with LC unfolding and protein conduction through the TD channel. Translocation occurs as a series of progressive steps in an N- to C-terminus orientation; productive completion requires reduction of the disulfide bridge and proteolytic cleavage of the LC from the HC concurrent with LC refolding in the cytosol. The progressive, tight interplay between the individual domains inherent in the mechanism of BoNT intoxication resolve it as an elegant modular nanomachine.

ISBN: 9780549337188Subjects--Topical Terms:

1019105
Biophysics, General.

Chaperone function of the botulinum neurotoxin protein translocating channel.
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020 $a 9780549337188
035 $a (UMI)AAI3289445
035 $a AAI3289445
040 $a UMI $c UMI
100 1 $a Fischer, Audrey. $3 1025704
245 1 0 $a Chaperone function of the botulinum neurotoxin protein translocating channel.
300 $a 190 p.
500 $a Adviser: Mauricio Montal.
500 $a Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7181.
502 $a Thesis (Ph.D.)--University of California, San Diego, 2008.
520 $a Clostridial botulinum neurotoxins (BoNTs) induce neuroparalysis by arresting synaptic exocytosis. BoNT consists of three functional domains: protease, translocation and receptor binding, and is cleaved into two disulfide linked, polypeptide chains: Light chain (LC) protease and Heavy chain (HC) translocon and receptor binding. One of the most elusive and intriguing steps of the BoNT intoxication process is the translocation of the proteolytic LC through the BoNT protein-conducting channel of the HC, from the endosomal compartment to the cytosol. In this dissertation, we utilize single-particle electron microscopy to resolve the discrepancies in multi-domain arrangement between different isoforms of BoNT in an effort to visualize rearrangement of domains and conformational changes associated with the translocation process. We investigate the dynamics of protein-translocation focusing on the interactions between the HC channel/chaperone and its LC cargo. Single molecule translocation was monitored in real time using excised patches of neuronal cells. LC translocation requires translocation domain (TD) insertion in a receptor binding domain (RBD) dependent manner, coupled with LC unfolding and protein conduction through the TD channel. Translocation occurs as a series of progressive steps in an N- to C-terminus orientation; productive completion requires reduction of the disulfide bridge and proteolytic cleavage of the LC from the HC concurrent with LC refolding in the cytosol. The progressive, tight interplay between the individual domains inherent in the mechanism of BoNT intoxication resolve it as an elegant modular nanomachine.
590 $a School code: 0033.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 $a University of California, San Diego. $b Biology. $3 1020228
773 0 $t Dissertation Abstracts International $g 68-11B.
790 $a 0033
790 1 0 $a Hampton, Randy $e committee member
790 1 0 $a Montal, Mauricio, $e advisor
790 1 0 $a Okamura, Melvin $e committee member
790 1 0 $a Schroeder, Julian $e committee member
790 1 0 $a Young, John $e committee member
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3289445