Zobrazeno 1 - 10
of 21
pro vyhledávání: '"P J, Bassford"'
Publikováno v:
Journal of Biological Chemistry. 268:20855-20862
The folding of maltose-binding protein, a periplasmic protein in Escherichia coli, was shown to proceed through the same rate-limiting step whether folding occurred in the cell under physiological conditions or in vitro in the absence of other protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::495deb03333ba8ef3c0987fe5a3b27d3
https://doi.org/10.1016/s0021-9258(19)36864-4
https://doi.org/10.1016/s0021-9258(19)36864-4
Publikováno v:
The Journal of biological chemistry. 269(18)
Signal peptidase I (also called leader peptidase) is the endopeptidase that removes the signal peptides of most secreted proteins during or after translocation in Escherichia coli. Precursor recognition is contingent in part on the presence of small,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7fad67fc79a5980cd0c879899728d8e1
https://pubmed.ncbi.nlm.nih.gov/8175796
https://pubmed.ncbi.nlm.nih.gov/8175796
Autor:
G A, Barkocy-Gallagher, P J, Bassford
Publikováno v:
The Journal of biological chemistry. 267(2)
The residues occupying the -3 and -1 positions relative to the cleavage site of secretory precursor proteins are usually amino acids with small, neutral side chains that are thought to constitute the recognition site for the processing enzyme, signal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9f2cfd39db3f9bf68e7b41acd6a9d1ea
https://pubmed.ncbi.nlm.nih.gov/1730647
https://pubmed.ncbi.nlm.nih.gov/1730647
Publikováno v:
The Journal of biological chemistry. 265(6)
Comparative analyses of a number of secretory proteins processed by eukaryotic and prokaryotic signal peptidases have identified a strongly conserved feature regarding the residues positioned -3 and -1 relative to the cleavage site. These 2 residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b5e04868dfe7c207264a37d033cbc95a
https://pubmed.ncbi.nlm.nih.gov/2406254
https://pubmed.ncbi.nlm.nih.gov/2406254
Autor:
P J Bassford, J P Ryan
Publikováno v:
Journal of Biological Chemistry. 260:14832-14837
We have studied the export kinetics of the maltose-binding protein (MBP) of Escherichia coli, the malE gene product, when it is synthesized with either a wildtype signal sequence or with a mutationally altered signal sequence that affects the efficie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12d30cc6847a5cfbed1c554b8da4d154
https://doi.org/10.1016/s0021-9258(17)38647-7
https://doi.org/10.1016/s0021-9258(17)38647-7
Publikováno v:
Journal of Biological Chemistry. 260:9727-9733
Maltose-binding protein (MBP) is essential for maltose transport and chemotaxis in Escherichia coli. To perform these functions it must interact with two sets of cytoplasmic membrane proteins, the MalFGK transport complex and the chemotactic signal t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41dccddf10c5e35e7e5c92974b88dbfb
https://doi.org/10.1016/s0021-9258(17)39299-2
https://doi.org/10.1016/s0021-9258(17)39299-2
Autor:
P J Bassford, B A Rasmussen
Publikováno v:
Journal of Bacteriology. 161:258-264
It previously has been demonstrated that synthesis of the periplasmic maltose-binding protein (MBP) and alkaline phosphatase (AP) of Eschericha coli predominantly occurs on membrane-bound polysomes. In this study, signal sequence alterations that adv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed2a3cb8e779f54b1caaf459ac6c4a3
https://doi.org/10.1128/jb.161.1.258-264.1985
https://doi.org/10.1128/jb.161.1.258-264.1985
Publikováno v:
Journal of Bacteriology. 129:265-275
The bfe locus codes for the cell surface receptor for vitamin B12, the E colicins, and bacteriophage BF23 in the Escherichia coli outer membrane. When the bfe+ allele, which is closely linked to the argH locus, was introduced into an argH bfe recipie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99ef32efd967743607b7bd439613ef4b
https://doi.org/10.1128/jb.129.1.265-275.1977
https://doi.org/10.1128/jb.129.1.265-275.1977
Publikováno v:
Journal of Bacteriology. 130:750-758
The expression of several functional properties of the products of the bfe and tonB genes in Escherichia coli was measured after the specific termination of the synthesis of the products of these genes. This was accomplished by the use of a temperatu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88dfd2a5f7beb3ef7270b4e2d1444bbf
https://doi.org/10.1128/jb.130.2.750-758.1977
https://doi.org/10.1128/jb.130.2.750-758.1977
Publikováno v:
Journal of Bacteriology. 159:1077-1079
The export of fimbrial subunits was found to be diminished at the restrictive temperature in a strain bearing a secA(Ts) mutation. Likewise, export was inhibited in a strain harboring a malE-lacZ protein fusion upon induction of hybrid protein synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7500a9be6906273d672abdb41ce87e97
https://doi.org/10.1128/jb.159.3.1077-1079.1984
https://doi.org/10.1128/jb.159.3.1077-1079.1984