Disordered regions endow structural flexibility to shell proteins and function towards shell–enzyme interactions in 1,2-propanediol utilization microcompartment

Abstract

Intrinsically disordered regions in proteins have been functionally linked to the protein–protein interactions and genesis of several membraneless organelles. Depending on their residual makeup, hydrophobicity or charge distribution they may remain in extended form or may assume certain conformations upon biding to a partner protein or peptide. The present work investigates the distribution and potential roles of disordered regions in the integral proteins of 1,2-propanediol utilization microcompartments. We use bioinformatics tools to identify the probable disordered regions in the shell proteins and enzyme of the 1,2-propanediol utilization microcompartment. Using a combination of computational modelling and biochemical techniques we elucidate the role of disordered terminal regions of a major shell protein and enzyme. Our findings throw light on the importance of disordered regions in the self-assembly, providing flexibility to shell protein and mediating its interaction with a native enzyme.

Communicated by Ramaswamy H. Sarma

Keywords:

• Bacterial microcompartment
• intrinsically disordered regions
• shell protein
• limited proteolysis

Acknowledgements

The authors thank S.S Lab members for helpful discussions. G.K thanks INST Mohali for fellowship.

Disclosure statement

The authors declare that they have no competing interests.

Data availability statement

All data generated or analyzed during this study are included in this article and its supporting information.

Additional information

Funding

This work was supported by DBT grant BT/12/IYBA/2019/08 to S.S.