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The Accessory SecA ATPase

Verburg, I. (2011) The Accessory SecA ATPase. Bachelor's Thesis, Biology.

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In bacterial pathogens, the majority of the virulence factors are extracytoplasmic proteins exported to the cell surface or secreted further into the extracellular environment. The general secretion (Sec) pathway is responsible for the translocation of the majority of proteins in bacteria. This translocation is performed by the Sec-translocase, which, in its minimal form, consists of SecYEG and SecA. The SecA ATPase functions as an motor protein that drives the protein trough the SecYEG channel by undergoing conformational changes upon ATP binding and hydrolysis. The SecA protein is essential for viability in all bacteria tested so far. In some, mostly pathogenic Gram-positive bacteria and mycobacteria, an additional SecA homologue is found. This accessory SecA is not essential for viability but has shown to play an important role in bacterial pathogenesis. Some of these additional SecA systems include an accessory SecY protein as well. The exact function and mechanism of these systems is not entirely understood. In this work the current understanding of the accessory SecA is summarized and the differences and similarities found between the various SecA systems are described and evaluated.

Item Type: Thesis (Bachelor's Thesis)
Degree programme: Biology
Thesis type: Bachelor's Thesis
Language: English
Date Deposited: 15 Feb 2018 07:45
Last Modified: 15 Feb 2018 07:45

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