TY - JOUR
T1 - Sequence information within the lamB gene is required for proper routing of the bacteriophage λ receptor protein to the outer membrane of Escherichia coli K-12
AU - Hall, Michael N.
AU - Schwartz, Maxime
AU - Silhavy, Thomas J.
N1 - Funding Information:
This work was supported by grant CM 25524 from the National Institute of General Medical Sciences and grant 77.7.1294 from the Delegation Generale it la Recherche Scientifique et Technique. This research was sponsored by the National Cancer Institute, Department of Health and Human Services, under contract no. NOl-CO-75380 with Litton Bionetics, Inc. The contents of this publication do not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products or organizations imply endorsement hy the United States government.
PY - 1982/3/25
Y1 - 1982/3/25
N2 - A series of hybrid genes has been constructed by fusion of the gene (lamB) coding for the outer membrane λ receptor protein (LamB), and the gene coding for the cytoplasmic enzyme β-galactosidase, lacZ. The resultant hybrid proteins of this series contain varying amounts of LamB at the NH2 terminus and a constant amount of functional β-galactosidase at the COOH terminus. The amount of lamB-coded protein present varies from two to about 270 amino acids of the 450 amino acids found in the mature LamB protein. The largest hybrid protein is novel, exhibiting several unique properties. It is efficiently localized to the outer membrane, exhibits an extremely low β-galactosidase specific activity, and is insoluble in Triton X-100. Other hybrid proteins, containing shorter LamB sequences, are localized less efficiently or not at all. The results suggest that additional information within LamB, residing downstream from the NH2-terminal signal sequence, is required for proper routing of the protein to the outer membrane.
AB - A series of hybrid genes has been constructed by fusion of the gene (lamB) coding for the outer membrane λ receptor protein (LamB), and the gene coding for the cytoplasmic enzyme β-galactosidase, lacZ. The resultant hybrid proteins of this series contain varying amounts of LamB at the NH2 terminus and a constant amount of functional β-galactosidase at the COOH terminus. The amount of lamB-coded protein present varies from two to about 270 amino acids of the 450 amino acids found in the mature LamB protein. The largest hybrid protein is novel, exhibiting several unique properties. It is efficiently localized to the outer membrane, exhibits an extremely low β-galactosidase specific activity, and is insoluble in Triton X-100. Other hybrid proteins, containing shorter LamB sequences, are localized less efficiently or not at all. The results suggest that additional information within LamB, residing downstream from the NH2-terminal signal sequence, is required for proper routing of the protein to the outer membrane.
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U2 - 10.1016/0022-2836(82)90461-2
DO - 10.1016/0022-2836(82)90461-2
M3 - Article
C2 - 6212690
AN - SCOPUS:0020332958
SN - 0022-2836
VL - 156
SP - 93
EP - 112
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -