Pores in the outer membrane of Escherichia coli K12 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1978-01

AUTHORS

Wim van Alphen, Nelke van Selm, Ben Lugtenberg

ABSTRACT

Mutants lacking outer membrane proteins were studied in order to investigate the role of these proteins in the functioning of aqueous pores through the outer membrane. Protein b is involved in the functioning of pores through which low concentrations of adenosine-monophosphate (AMP), guanosine-monophosphate (GMP), bis(paranitrophenyl)-phosphate (bis-PNPP) and, although less pronounced, also cytidine-monophosphate (CMP) enter the cell. In the absence of the receptor protein of phage T6, which facilitates the permeation of various nucleosides (Hantke, 1976), protein b plays a major role in the uptake of adenosine. Proteins c and d and the receptor proteins of phages lambda and T6 do not have a pore function for AMP, GMP, CMP and bis-PNPP. However, a newly discovered peptidoglycan-associated protein, protein e, can also mediate the permeation of the latter four components, but not of adenosine, through the outer membrane. Protein b does not play a major role in the uptake of higher concentrations of AMP. Obviously mainly other pores are used under those conditions. The results strongly suggest that at low concentrations of nucleoside monophosphates (and possibly of other nutrients) protein b functions as a specific pore. More... »

PAGES

75-83

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00401750

DOI

http://dx.doi.org/10.1007/bf00401750

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042872827

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/204859


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