Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/136087
Title: STRUCTURE AND FUNCTION OF ACTIN-LIKE PROTEINS IN CLOSTRIDIA
Authors: KOH FUJIET
Keywords: cytoskeleton,bactera,clostridia,structure,cryoEM,ParM
Issue Date: 20-Jan-2017
Source: KOH FUJIET (2017-01-20). STRUCTURE AND FUNCTION OF ACTIN-LIKE PROTEINS IN CLOSTRIDIA. ScholarBank@NUS Repository.
Abstract: In this thesis, potential ParMRC systems from several infamously pathogenic Clostridia bacteria, such as Clostridium botulinum and Clostridium tetani were characterised. ParMRC40 from Clostridium botulinum was found to segregate plasmids carrying BoNT A, which encodes for botulinum toxin A, and an 8.8 Å cryoEM structure of the highly complex CB-ParM40 has been solved. ParMRC12 from Clostridium tetani segregates several plasmids which harbours the gene encoding for tetanospasmin. A cryoEM dataset for CT-ParM12 is collected and characterised. Lastly, ParMRC20 from Clostridium botulinum was found to segregate plasmids containing a wide variety of virulence factors. The structure of CB-ParM20 was solved to 4.5 Å. This work demonstrates the wide range of filamentous structures probed during the evolution of bacterial actin-like proteins. In the absence of the selective pressure to bind to the many different actin-binding proteins, as in the case of eukaryotes, prokaryotes have developed a wider repertoire of actin-fold based structures.
URI: http://scholarbank.nus.edu.sg/handle/10635/136087
Appears in Collections:Ph.D Theses (Restricted)

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