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The ins and outs of Bacillus proteases: activities, functions and commercial significance

Lookup NU author(s): Emeritus Professor Colin Harwood

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

Because the majority of bacterial species divide by binary fission, and do not have distinguishable somatic and germ-lines cells, they could be considered to be immortal. However, bacteria “age” due to damage to vital cell components such as DNA and proteins. DNA damage can often be repaired using efficient DNA repair mechanisms. However, many proteins have a functional “shelf life”; some short lived, others are relatively stable. Specific degradation processes are built into the life span of proteins whose activities are required to fulfil a specific function during a prescribed period of time (e.g. cell cycle, differentiation process, stress response). In addition, proteins that are irreparably damaged or that have come to the end of their functional lifespan need to be removed by quality control proteases. Other proteases perform a variety of functions that can be broadly divided in to three categories: processing, regulation and feeding. This review presents a systematic account of the proteases of Bacillus subtilis and their activities. It reviews the proteases found in, or associated with, the cytoplasm, the cell membrane, the cell wall and the external milieu. Where known, the impacts of the deletion of particular proteases are discussed, particular in relation to industrial applications.

Publication metadata

Author(s): Harwood CR, Kikuchi Y

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Reviews

Year: 2022

Volume: 46

Issue: 1

Print publication date: 01/01/2022

Online publication date: 19/08/2021

Acceptance date: 17/08/2021

Date deposited: 06/09/2021

ISSN (print): 0168-6445

ISSN (electronic): 1574-6976

Publisher: Oxford University Press

URL: https://doi.org/10.1093/femsre/fuab046

DOI: 10.1093/femsre/fuab046

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