Journal
MOLECULAR MICROBIOLOGY
Volume 106, Issue 5, Pages 760-776Publisher
WILEY
DOI: 10.1111/mmi.13844
Keywords
-
Categories
Funding
- JSPS KAKENHI [JP15H04350, JP15K07008, JP26291023]
- MEXT KAKENHI [JP15H01532, JP26119007, JP17H05669, JP15H01537]
- Asahi Glass Foundation
- Platform for Drug Discovery, Informatics, and Structural Life Science - Ministry of Education, Culture, Sports, Science and Technology, Japan
- Australian Research Council [DP160100227]
- Grants-in-Aid for Scientific Research [15H04350, 26119007, 15K06972, 17H05666, 17H05879, 15K07008, 16K14713] Funding Source: KAKEN
Ask authors/readers for more resources
BepA (formerly YfgC) is an Escherichia coli periplasmic protein consisting of an N-terminal protease domain and a C-terminal tetratricopeptide repeat (TPR) domain. We have previously shown that BepA is a dual functional protein with chaperone-like and proteolytic activities involved in membrane assembly and proteolytic quality control of LptD, a major component of the outer membrane lipopolysaccharide translocon. Intriguingly, BepA can associate with the BAM complex: the -barrel assembly machinery (BAM) driving integration of -barrel proteins into the outer membrane. However, the molecular mechanism of BepA function and its association with the BAM complex remains unclear. Here, we determined the crystal structure of the BepA TPR domain, which revealed the presence of two subdomains formed by four TPR motifs. Systematic site-directed in vivo photo-cross-linking was used to map the protein-protein interactions mediated by the BepA TPR domain, showing that this domain interacts both with a substrate and with the BAM complex. Mutational analysis indicated that these interactions are important for the BepA functions. These results suggest that the TPR domain plays critical roles in BepA functions through interactions both with substrates and with the BAM complex. Our findings provide insights into the mechanism of biogenesis and quality control of the outer membrane.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available