TY - JOUR
T1 - Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
AU - Sklar, Joseph G.
AU - Wu, Tao
AU - Gronenberg, Luisa S.
AU - Malinverni, Juliana C.
AU - Kahne, Daniel
AU - Silhavy, Thomas J.
PY - 2007/4/10
Y1 - 2007/4/10
N2 - A major role of the outer membrane (OM) of Gram-negative bacteria is to provide a protective permeability barrier for the cell, and proper maintenance of the OM is required for cellular viability. OM biogenesis requires the coordinated assembly of constituent lipids and proteins via dedicated OM assembly machineries. We have previously shown that, in Escherichia coli, the multicomponent YaeT complex is responsible for the assembly of OM β-barrel proteins (OMPs). This complex contains the OMP YaeT and three OM lipoproteins. Here, we report another component of the YaeT complex, the OM lipoprotein small protein A (SmpA). Strains carrying loss-of-function mutations in smpA are viable but exhibit defects in OMP assembly. Biochemical experiments show that SmpA is involved in maintaining complex stability. Taken together, these experiments establish an important role for SmpA in both the structure and function of the YaeT complex.
AB - A major role of the outer membrane (OM) of Gram-negative bacteria is to provide a protective permeability barrier for the cell, and proper maintenance of the OM is required for cellular viability. OM biogenesis requires the coordinated assembly of constituent lipids and proteins via dedicated OM assembly machineries. We have previously shown that, in Escherichia coli, the multicomponent YaeT complex is responsible for the assembly of OM β-barrel proteins (OMPs). This complex contains the OMP YaeT and three OM lipoproteins. Here, we report another component of the YaeT complex, the OM lipoprotein small protein A (SmpA). Strains carrying loss-of-function mutations in smpA are viable but exhibit defects in OMP assembly. Biochemical experiments show that SmpA is involved in maintaining complex stability. Taken together, these experiments establish an important role for SmpA in both the structure and function of the YaeT complex.
UR - http://www.scopus.com/inward/record.url?scp=34547512065&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34547512065&partnerID=8YFLogxK
U2 - 10.1073/pnas.0701579104
DO - 10.1073/pnas.0701579104
M3 - Article
C2 - 17404237
AN - SCOPUS:34547512065
SN - 0027-8424
VL - 104
SP - 6400
EP - 6405
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 - 15
ER -