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Pore protein e of the outer membrane of escherichia coli K12
Author(s) -
Lugtenberg Ben,
Boxtel Ria van,
Verhoef Cornelis,
Alphen Wim van
Publication year - 1978
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(78)81071-0
Subject(s) - cell and molecular biology , molecular cell biology , biology , library science , microbiology and biotechnology , genetics , computer science , gene , plant development
Several outer membrane proteins of Gram-negative bacteria function in the formation of pores through which nutrients and other solutes pass the outer membrane. General pores facilitate the permeation of a large number of structurally unrelated solutes through the outer membrane whereas other pores are used by one or only a few structurally related solutes. An extensive description of the properties of various pores can be found in [l-l 21. The peptidoglycanassociated proteins b and c (nomenclature of [ 131) are involved in the functioning of general pores [7,8,10,1 I] in wild type strains ofEscherichiu coli K12. The purification and partial characterization of these proteins have been described extensively [ 14&19]. Recently we described that another peptidoglycan-associated protein, protein e, which was detected in pseudo-revertants of mutants lacking proteins b and c (b-cmutants), is also involved in the functioning of pores [lo]. The isolation and properties of e+ mutants and a comparison of the purified protein e with proteins b and c is described here. Moreover we will show that protein e and the proteins Ic [ 161 and E [20] are identical.