Javascript must be enabled for the correct page display

Interaction between PBP2b and DivIB in Bacillus subtilis

Maciá Valero, Alicia (2019) Interaction between PBP2b and DivIB in Bacillus subtilis. Research Project 2, Molecular Biology and Biotechnology.

[img]
Preview
Text
Report - Alicia Macia Valero - final.pdf

Download (2MB) | Preview
[img] Text
toestemming.pdf
Restricted to Registered users only

Download (141kB)

Abstract

The cell wall is an essential component for bacterial cells, which provides them with shape, integrity, protection from the environment and osmotic pressure shocks, and a scaffold for anchoring of other proteins. Synthesis of the main component, peptidoglycan, is mediated by a complex of different proteins during cell division and elongation. One of those proteins, PBP2b, essential in Bacillus subtilis, is recruited to the division site by DivIB in order to perform the transpeptidase activity responsible for cross-linking of peptidoglycan. The interaction between DivIB and PBP2b has been demonstrated in the past. However, details about that interaction such as the orientation or residues involved are yet to be deciphered. PBP2b contains two PASTA domains in the sequence whose function is hitherto unknown. In this work, it is demonstrated by co-immunoprecipitation assays and observation under the microscope that deletion of PBP2b PASTA domains negatively affects the DivIB-PBP2b interaction. Together with previous bacterial two hybrid experiments from the group, these results suggest that, although not exclusively, PASTA domains from PBP2b are involved in the DivIB-PBP2b interaction and most likely stabilize it, improving the efficiency of PBP2b recruitment to the division site during cell wall biosynthesis.

Item Type: Thesis (Research Project 2)
Supervisor:
Supervisor nameSupervisor E mail
Scheffers, D.J.D.J.Scheffers@rug.nl
Degree programme: Molecular Biology and Biotechnology
Thesis type: Research Project 2
Language: English
Date Deposited: 21 Aug 2019
Last Modified: 23 Aug 2019 12:19
URI: http://fse.studenttheses.ub.rug.nl/id/eprint/20726

Actions (login required)

View Item View Item