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Regulation of the anti-sigma factor ...
~
Calvo, Rebecca Ann.
Regulation of the anti-sigma factor FlgM in Bacillus subtilis.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
書名/作者:
Regulation of the anti-sigma factor FlgM in Bacillus subtilis.
作者:
Calvo, Rebecca Ann.
面頁冊數:
238 p.
附註:
Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.
Contained By:
Dissertation Abstracts International76-10B(E).
標題:
Microbiology.
標題:
Genetics.
ISBN:
9781321815085
摘要、提要註:
Many bacteria are motile and propel themselves by rotating one or more flagella. The flagellar filament is composed of ∼20,000 subunits of a single protein (Flagellin). The filament is polymerized atop an intricate membrane-embedded structure called the hook and basal body (HBB). The HBB localizes a dedicated flagellar type III secretion apparatus, the activity of which is regulated so that the timing of flagellar protein secretion across the cytoplasmic membrane results in the ordered assembly of the flagellum. The type III secretion apparatus recognizes two classes of secretion substrates: rod/hook-type substrates and filament-type substrates.
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3707125
Regulation of the anti-sigma factor FlgM in Bacillus subtilis.
Calvo, Rebecca Ann.
Regulation of the anti-sigma factor FlgM in Bacillus subtilis.
- 238 p.
Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.
Thesis (Ph.D.)--Indiana University, 2015.
Many bacteria are motile and propel themselves by rotating one or more flagella. The flagellar filament is composed of ∼20,000 subunits of a single protein (Flagellin). The filament is polymerized atop an intricate membrane-embedded structure called the hook and basal body (HBB). The HBB localizes a dedicated flagellar type III secretion apparatus, the activity of which is regulated so that the timing of flagellar protein secretion across the cytoplasmic membrane results in the ordered assembly of the flagellum. The type III secretion apparatus recognizes two classes of secretion substrates: rod/hook-type substrates and filament-type substrates.
ISBN: 9781321815085Subjects--Topical Terms:
182563
Microbiology.
Regulation of the anti-sigma factor FlgM in Bacillus subtilis.
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Source: Dissertation Abstracts International, Volume: 76-10(E), Section: B.
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Adviser: Daniel B. Kearns.
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Many bacteria are motile and propel themselves by rotating one or more flagella. The flagellar filament is composed of ∼20,000 subunits of a single protein (Flagellin). The filament is polymerized atop an intricate membrane-embedded structure called the hook and basal body (HBB). The HBB localizes a dedicated flagellar type III secretion apparatus, the activity of which is regulated so that the timing of flagellar protein secretion across the cytoplasmic membrane results in the ordered assembly of the flagellum. The type III secretion apparatus recognizes two classes of secretion substrates: rod/hook-type substrates and filament-type substrates.
520
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Transcription of flagellar genes is morphogenetically coupled to the assembly state of the nascent flagellum. HBB genes are transcribed by the housekeeping sigma factor sigmaA and the flagellin gene is transcribed by the alternative sigma factor sigma D. Prior to HBB completion, sigmaD is inhibited by the anti-sigma factor FlgM that binds to sigmaD in the cytoplasm to prevent it from activating transcription. During HBB assembly, the type III secretion apparatus recognizes and secretes rod/hook-type substrates. Completion of the HBB alters the type III secretion apparatus to recognize and secrete filament-type substrates, including the anti-sigma factor FlgM. Secretion of FlgM liberates sigmaD in the cytoplasm to transcribe flagellin, which is subsequently translated and secreted by the type III secretion apparatus to be assembled onto the distal end of the nascent flagellum. The temporal control of flagellin transcription by FlgM is important because it ensures that cells only express flagellin once the HBB structure is complete.
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This work demonstrates that regulation of FlgM activity in the Gram-positive bacterium Bacillus subtilis largely conforms to the FlgM secretion model of morphogenetic coupling. By using cytological, forward, and molecular genetic approaches, this work comprehensively tests the secretion model and characterizes the FlgM:sigmaD complex in B. subtilis. This work defines a minimum set of nine HBB proteins strictly required for FlgM secretion and identifies two specific proteases that degrade FlgM in the extracellular environment. Finally, this work highlights an important difference in FlgM regulation in B. subtilis and examines the role of FlgM in the context of other regulators of sigma D.
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