Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.753091
Title: Genetic, biochemical and structural characterisation of YecA, a novel component of the bacterial Sec machinery
Author: Cranford-Smith, Tamar
ISNI:       0000 0004 7426 1983
Awarding Body: University of Birmingham
Current Institution: University of Birmingham
Date of Award: 2018
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Abstract:
The Sec pathway provides a mechanism for the translocation of proteins across or into the cytoplasmic membrane. In bacteria, SecA is a core component of the Sec machinery. YecA has a 20-amino acid sequence at its carboxy-terminus that has high sequence identity to the zinc-binding domain at the carboxy-terminus of SecA. This study provides evidence to show that YecA is a novel component of the Sec machinery of E. coli. The yecA gene is not essential for the viability of E. coli but the deletion of yecA interferes with Sec-dependent translocation and the combined deletion of the yecA and secB genes results in a severely cold-sensitive phenotype. The genetic investigations were supported by biochemical evidence that suggests that YecA improves the translocation-coupled ATPase activity of SecA. Structural investigations suggest that YecA is a monomer in solution. The α-helical domain that forms the main body of YecA is connected via a short linker with limited flexibility to an independent metal-binding domain that has two conformations. The purification of YecA suggested the presence of iron. Biophysical experiments were used to confirm the interaction of the YecA metal-binding domain with iron. This study provides evidence for an additional component of the translocation machinery.
Supervisor: Not available Sponsor: Biotechnology and Biological Sciences Research Council (BBSRC) ; Microbiology Society
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.753091  DOI: Not available
Keywords: QR Microbiology
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