A structural insight into Bacterial Microcompartments and the mechanism of cargo encapsulation.
Lead Research Organisation:
Queen Mary University of London
Department Name: Sch of Biological and Chemical Sciences
Abstract
Strategic Research Priority: World Class Bioscience
Aim to investigate the role of N- terminal extension peptides present in a number of enzymes sequestered within BMCs (Bacterial Microcompartments), how they interact with specific shell proteins and enable the encapsulation of non native cargo. Detailed structural information is available for the majority of Pdu (Propanediol) utilisation Microcompartment shell proteins, however the shell protein PduK has so far evaded crystallisation. PduK features a C- terminal extension which is not homologous to any other known fold, additionaly PduK interacts with Rubisco via its C- terminus through an unknown mechanism, elucidation of this and the structure of the PduK C- terminus would be beneficial.
Aim to investigate the role of N- terminal extension peptides present in a number of enzymes sequestered within BMCs (Bacterial Microcompartments), how they interact with specific shell proteins and enable the encapsulation of non native cargo. Detailed structural information is available for the majority of Pdu (Propanediol) utilisation Microcompartment shell proteins, however the shell protein PduK has so far evaded crystallisation. PduK features a C- terminal extension which is not homologous to any other known fold, additionaly PduK interacts with Rubisco via its C- terminus through an unknown mechanism, elucidation of this and the structure of the PduK C- terminus would be beneficial.
Publications
Uddin I
(2018)
A Generic Self-Assembly Process in Microcompartments and Synthetic Protein Nanotubes.
in Small (Weinheim an der Bergstrasse, Germany)
Studentship Projects
| Project Reference | Relationship | Related To | Start | End | Student Name |
|---|---|---|---|---|---|
| BB/M009513/1 | 01/10/2015 | 31/03/2024 | |||
| 1786255 | Studentship | BB/M009513/1 | 01/10/2016 | 30/09/2020 | Jack Bradley-Clarke |
| Description | Previous reseach has identified N- terminal signaling peptides on the cargo enzymes found within Bacterial microcomparmtents are responsible for their packaging into the comparmtent lumen. The precise manner in which these enzymes interact with shell proteins has remained elusive for some time, knowledge of the manner of this interaction and specificifity would allow for packaging of complex, non- native enzymatic pathways into microcomparmtents. In the course of this project, the location and mechanism of the signalling peptide- shell protein interaction has been established. This data was written up and submitted to PNAS, whilst the manuscript was rejected they indicated this was due to a lack of concrete evidence. Various mutagenic experiments have been completed over the last year to further support the model which was previously proposed and the manuscript will be ammended and re- submitted in the near future. |
| Exploitation Route | Previous attempts to incorporate non- native cargo enymes into the microcompartment lumen have shown increased substrate transfer between simple two enzyme systems, leading to increased catalytic rates. Now a precise mechanism for cargo encapsulation is known, larger more complex metabolic pathways could potentially be encapsulated, with different amounts of these enzymes present. This could be very useful for enhancing the yields of industrial applications which use multi enzyme pathways. |
| Sectors | Chemicals,Manufacturing, including Industrial Biotechology |