학술논문

Bacterial secretion chaperones: the mycobacterial type VII case
Physiology & Biochemistry
Document Type
Report
Source
FEMS Microbiology Letters. September 15, 2018, Vol. 365 Issue 18, p1j, 8 p.
Subject
Netherlands
Language
English
ISSN
0378-1097
Abstract
INTRODUCTION Chaperones are an important group of proteins that play key roles in cellular homeostasis by assisting in protein folding, multimeric protein assembly, protein trafficking and protein degradation. In prokaryotes, [...]
Chaperones are central players in maintaining the proteostasis in all living cells. Besides highly conserved generic chaperones that assist protein folding and assembly in the cytosol, additional more specific chaperones have evolved to ensure the successful trafficking of proteins with extra-cytoplasmic locations. Associated with the distinctive secretion systems present in bacteria, different dedicated chaperones have been described that not only keep secretory proteins in a translocation competent state, but often are also involved in substrate targeting to the specific translocation channel. Recently, a new class of such chaperones has been identified that are involved in the specific recognition of substrates transported via the type VII secretion pathway in mycobacteria. In this minireview, we provide an overview of the different bacterial chaperones with a focus on their roles in protein secretion and will discuss in detail the roles of mycobacterial type VII secretion chaperones in substrate recognition and targeting. Keywords: chaperone; substrate recognition; protein targeting; protein secretion; type VII secretion; mycobacterium