Journal
MOLECULAR MICROBIOLOGY
Volume 59, Issue 2, Pages 487-502Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1365-2958.2005.04968.x
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM53989, GM18568] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM018568, R29GM053989, R37GM018568, R01GM053989] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Bacterial spores are surrounded by a morphologically complex, mechanically flexible protein coat, which protects the spore from toxic molecules. The interactions among the over 50 proteins that make up the coat remain poorly understood. We have used cell biological and protein biochemical approaches to identify novel coat proteins in Bacillus subtilis and describe the network of their interactions, in order to understand coat assembly and the molecular basis of its protective functions and mechanical properties. Our analysis characterizes the interactions between 32 coat proteins. This detailed view reveals a complex interaction network. A key feature of the network is the importance of a small subset of proteins that direct the assembly of most of the coat. From an analysis of the network topology, we propose a model in which low-affinity interactions are abundant in the coat and account, to a significant degree, for the coat's mechanical properties as well as structural variation between spores.
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