Use this URL to cite or link to this record in EThOS:
Title: Analysis of the accessory Sec systems in streptococcus
Author: Bandara, Mikaila Jayaweera
ISNI:       0000 0004 5917 2499
Awarding Body: University of Bristol
Current Institution: University of Bristol
Date of Award: 2015
Availability of Full Text:
Access from EThOS:
The bulk of protein secretion in bacteria occurs through the general secretion (Sec) pathway. Proteins interact via their N-terminal leader peptides with the membrane-associated Sec system where they undergo processing, secretion and folding within the cell wall environment. Some Gram-positive bacteria and mycobacteria have been shown to possess a second Sec pathway known as the accessory Sec system. This exports proteins with specific N-terminalleader peptides and assists in the secretion of other proteins that lack N-terminal leaders. The core component of this system is SecA'2, a functional homologue of SecA in the canonical system. Other core components include SecY2 (homologue of SecY) and accessory Sec proteins Asp l-Asp5. The objective of this study was to characterise the composition and activities of the accessory Sec systems in commensal Streptococcus gordonii and pathogenic Streptococcus pneumoniae.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available