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pro vyhledávání: '"Charles F. Earhart"'
Autor:
Charles F. Earhart, Feras M. Hantash
Publikováno v:
Journal of Bacteriology. 182:1768-1773
The cytosolic proteins EntE, EntF, and EntB/G, which are Escherichia coli enzymes necessary for the final stage of enterobactin synthesis, are released by osmotic shock. Here, consistent with the idea that cytoplasmic proteins found in shockates have
Publikováno v:
Applied Microbiology and Biotechnology. 45:112-119
The Lpp'OmpA(46-159) hybrid protein can serve as an efficient targeting vehicle for localizing a variety of procaryotic and eucaryotic soluble proteins onto the E. coli surface, thus providing a system for several possible biotechnology applications.
Autor:
George Georgiou, Christos Stathopoulos, Daren L. Stephens, Heather L. Poetschke, John Mendenhall, Charles F. Earhart
Publikováno v:
"Protein Engineering, Design and Selection". 9:239-247
Bacterial cell-surface exposure of foreign peptides and soluble proteins has been achieved recently by employing a fusion protein methodology. An Lpp'-OmpA(46-159)-Bla fusion protein has been shown previously to display the normally periplasmic enzym
Autor:
J F Staab, Charles F. Earhart
Publikováno v:
Journal of Bacteriology. 172:6403-6410
The last steps in the biosynthesis of the Escherichia coli siderophore enterobactin (Ent) are carried out by Ent synthetase, a multienzyme complex believed to be composed of the entD, -E, -F, and -G products (EntD to -G). However, sequencing data sho
Autor:
Charles F. Earhart
Publisher Summary This chapter discusses the application of lipoprotein (Lpp)–OmpA fusion vehicle to study the surface of bacteria. The Lpp–OmpA vector is designed for use in the gram-negative bacterium Escherichia coli ; the rationale for its di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97586ddfc4f91b103d2bacee17dc4eb4
https://doi.org/10.1016/s0076-6879(00)26072-2
https://doi.org/10.1016/s0076-6879(00)26072-2
Publikováno v:
Microbiology (Reading, England). 143
The terminal reactions in the synthesis of the siderophore enterobactin (Ent) by Escherichia coli require the EntD, E, F and B/G polypeptides. The idea that these molecules form a complex (Ent synthase) that is membrane-associated was re-evaluated. I
Publikováno v:
Microbiology (Reading, England). 141
Summary: Most high-affinity systems for iron uptake in Gram-negative bacteria are thought to employ periplasmic-binding-protein-dependent transport. In Escherichia coli, FepB is a periplasmic protein required for uptake of iron complexed to its endog
Autor:
Charles F. Earhart, Sara S. Chenault
Publikováno v:
Journal of general microbiology. 138(10)
In Escherichia coli, iron assimilation by means of the siderophore enterobactin requires two hydrophobic cytoplasmic membrane proteins, FepD and FepG, which are essential components of a binding-protein-dependent transport system. Such components are
Autor:
Charles F. Earhart
Publikováno v:
Biology of Metals. 4:70-71
Autor:
M.D. Lundrigan, Charles F. Earhart
Publikováno v:
FEMS Microbiology Letters. 24:341-344
The outer membrane protein BtuB of Escherichia coli K-12 is the receptor for vitamin B12; it is normally present in approx. 200 copies per cell. We describe here the conditions by which BtuB was readily observed in electropherograms of outer membrane