TY - JOUR
T1 - Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control
AU - Shen, Qing Tao
AU - Bai, Xiao Chen
AU - Chang, Lei Fu
AU - Wu, Yi
AU - Wang, Hong Wei
AU - Sui, Sen Fang
PY - 2009/3/24
Y1 - 2009/3/24
N2 - In the periplasm of Escherichia coli, DegP (also known as HtrA), which has both chaperone-like and proteolytic activities, prevents the accumulation of toxic misfolded and unfolded polypeptides. In solution, upon binding to denatured proteins, DegP forms large cage-like structures. Here, we show that DegP forms a range of bowl-shaped structures, independent of substrate proteins, each with a 4-, 5-, or 6-fold symmetry and all with a DegP trimer as the structural unit, on lipid membranes. These membrane-bound DegP assemblies have the capacity to recruit and process substrates in the bowl chamber, and they exhibit higher proteolytic and lower chaperone-like activities than DegP in solution. Our findings imply that DegP might regulate its dual roles during protein quality control, depending on its assembly state in the narrow bacterial envelope.
AB - In the periplasm of Escherichia coli, DegP (also known as HtrA), which has both chaperone-like and proteolytic activities, prevents the accumulation of toxic misfolded and unfolded polypeptides. In solution, upon binding to denatured proteins, DegP forms large cage-like structures. Here, we show that DegP forms a range of bowl-shaped structures, independent of substrate proteins, each with a 4-, 5-, or 6-fold symmetry and all with a DegP trimer as the structural unit, on lipid membranes. These membrane-bound DegP assemblies have the capacity to recruit and process substrates in the bowl chamber, and they exhibit higher proteolytic and lower chaperone-like activities than DegP in solution. Our findings imply that DegP might regulate its dual roles during protein quality control, depending on its assembly state in the narrow bacterial envelope.
KW - Chaperone
KW - Cryo-electron microscopy
KW - HtrA
KW - Protease
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U2 - 10.1073/pnas.0811780106
DO - 10.1073/pnas.0811780106
M3 - Article
C2 - 19255437
AN - SCOPUS:63849240148
SN - 0027-8424
VL - 106
SP - 4858
EP - 4863
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -