Receptor for bacteriophage lambda of Escherichia coli forms larger pores in black lipid membranes than the matrix protein (porin).
TLDR
The receptor for phage lambda in Escherichia coli was isolated by cholate extraction and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and found that the pore characteristics were similar to those exhibited by the matrix protein (porin) and the lambda receptor showed a somewhat higher degree of cation specificity.Abstract:
The receptor for phage lambda in Escherichia coli was isolated by cholate extraction and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Protein bands corresponding to the monomer and the dimer were eluted from the gel and tested for their activity to inactivate phage lambda and to form pores in black lipid membranes. It was found that only the dimer inactivated phage lambda, whereas both the monomer and the dimer were active in forming pores. The pore characteristics were similar to those exhibited by the matrix protein (porin) (R. Benz, K. Janko, W. Boos, and P. Lauger, Biochim. Biophys. Acta 511:305--319, 1978). In comparison, the lambda receptor showed a somewhat higher degree of cation specificity, and its pore size was larger. Assuming that the thickness of the outer membrane is 7.5 nm and that the pore is an ideal hydrophilic channel, the pore diameter in vivo was estimated to be 1.6 nm for the lambda receptor and 1.2 nm for the matrix protein.read more
Citations
More filters
Journal ArticleDOI
Molecular basis of bacterial outer membrane permeability.
Hiroshi Nikaido,Martti Vaara +1 more
TL;DR: It is becoming increasingly clear that the outer membrane is very important in the physiology of gram-negative bacteria in making them resistant to host defense factors such as lysozyme, P-lysin, and various leukocyte proteins.
Journal ArticleDOI
Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria
Journal ArticleDOI
Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli.
K B Heller,E C Lin,T H Wilson +2 more
TL;DR: The observation and the insensitivity of the xylitol transport to low temperature suggest that the facilitator behaves as a membrane channel.
Journal ArticleDOI
Ion selectivity of gram-negative bacterial porins.
TL;DR: Zero-current potential measurements in the presence of salt gradients across lipid bilayer membranes containing individual porins gave results that were consistent with the conclusions drawn from the single-channel experiments, indicating that the ions were moving inside the pores in a fashion similar to their movement in the aqueous phase.
References
More filters
Journal ArticleDOI
A rapid, sensitive, and specific method for the determination of protein in dilute solution
TL;DR: This protein assay is described in which the sample is precipitated with trichloroacetic acid in the presence of sodium dodecylsulfate, filtered off on a Millipore membrane and stained with Amidoschwarz 10B, and its absorbance determined at 630 nm.
Journal ArticleDOI
Analysis of bacteriophage T7 early RNAs and proteins on slab gels
TL;DR: The RNAs and proteins specified by five early genes of bacteriophage T7 have been identified by electrophoresis on sodium dodecyl sulfate, polyacrylamide gels using a slab gel system in which 25 samples can be run simultaneously and then dried for autoradiography.
Journal ArticleDOI
The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts.
Harold C. Neu,Leon A. Heppel +1 more
TL;DR: A new method for releasing most of the inducible alkaline phosphatases and of the cyclic phosphodiesterase in high yield without greatly impairing the viability of the cells is developed.
Journal ArticleDOI
Characterization of the Major Envelope Protein from Escherichia coli REGULAR ARRANGEMENT ON THE PEPTIDOGLYCAN AND UNUSUAL DODECYL SULFATE BINDING
TL;DR: The major envelope protein from Escherichia coli has been purified by differential heat extraction in dodecyl sulfate and subsequently freed of the detergent, and its molecular weight agrees with that derived from the mobility of the major band observed in standard dodecYL sulfate gel electrophoretic analysis of unfractionated cell envelopes after treatment at 100°.
Journal ArticleDOI
Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli.
TL;DR: One of the major proteins of the outer membrane of Escherichia coli, the matrix protein (porin), has been isolated by detergent solubilisation and the findings are consistent with the assumption that the protein forms large aqueous channels in the membrane.
Related Papers (5)
Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli.
Mary Luckey,Hiroshi Nikaido +1 more
Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor.
S Szmelcman,M Hofnung +1 more