The Bacillus subtilis spore coat protein interaction network.
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.
Kim
Hosan
H
Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, USA.
Hahn
Marlene
M
Grabowski
Paul
P
McPherson
Derrell C
DC
Otte
Michele M
MM
Wang
Rong
R
Ferguson
Caitlin C
CC
Eichenberger
Patrick
P
Driks
Adam
A
D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D017353:Gene Deletion; D011485:Protein Binding; D013171:Spores, Bacterial
D001426:Bacterial Proteins