Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Philip J. Bassford"'
Publikováno v:
Journal of Biological Chemistry. 269:13609-13613
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=doi_________::9e987e1872ae7d50cd62d2362287e050
https://doi.org/10.1016/s0021-9258(17)36873-4
https://doi.org/10.1016/s0021-9258(17)36873-4
Publikováno v:
Biochemical and Biophysical Research Communications. 197:1154-1166
Processing of 37 precursor maltose-binding protein (preMBP) species by purified signal peptidase I (SPase I) was assayed. The in vitro reaction was inefficient compared to processing in Escherichia coli cells. The extent of preMBP processing in vitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e94ab9ea3fe33badc0a29f4f519d795b
https://doi.org/10.1006/bbrc.1993.2598
https://doi.org/10.1006/bbrc.1993.2598
Publikováno v:
The EMBO Journal. 12:879-888
The prlA/secY gene, which codes for an integral membrane protein component of the Escherichia coli protein export machinery, is the locus of the strongest suppressors of signal sequence mutations. We demonstrate that two exported proteins of E.coli,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d58fa91fc66cf37eff4242d1da1941c
https://doi.org/10.1002/j.1460-2075.1993.tb05728.x
https://doi.org/10.1002/j.1460-2075.1993.tb05728.x
Publikováno v:
Journal of Biological Chemistry. 267:1231-1238
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=doi_________::3fc627aa5a83ea814df3ba8c3a8bcd40
https://doi.org/10.1016/s0021-9258(18)48419-0
https://doi.org/10.1016/s0021-9258(18)48419-0
Publikováno v:
Infection and Immunity. 59:1521-1528
A clone expressing a 35.5-kDa recombinant treponemal protein was isolated from a genomic DNA library constructed from Treponema pallidum street strain 14. Polyclonal antiserum raised against the recombinant protein reacted with a corresponding native
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997649ec5d625c2218bc3ba654e8adeb
https://doi.org/10.1128/iai.59.4.1521-1528.1991
https://doi.org/10.1128/iai.59.4.1521-1528.1991
Publikováno v:
Journal of Bacteriology. 172:6875-6884
The efficient export of the Escherichia coli maltose-binding protein (MBP) is known to be SecB dependent, whereas ribose-binding protein (RBP) export is SecB independent. When the MBP and RBP signal peptides were exchanged precisely at the signal pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7093a30f0d80893a4ed47d3ce3cd8e
https://doi.org/10.1128/jb.172.12.6875-6884.1990
https://doi.org/10.1128/jb.172.12.6875-6884.1990
Autor:
Philip J. Bassford
Publikováno v:
Journal of Bioenergetics and Biomembranes. 22:401-439
The export of the maltose-binding protein (MBP), the malE gene product, to the periplasm of Escherichia coli cells has been extensively investigated. The isolation of strains synthesizing MalE-LacZ hybrid proteins led to a novel genetic selection for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1aee9935fa1b00f3889b57163c83c0f7
https://doi.org/10.1007/bf00763175
https://doi.org/10.1007/bf00763175
Publikováno v:
Journal of Bacteriology. 176:3397-3399
Maltose-binding protein (MBP) is translocated across the cytoplasmic membrane of Escherichia coli; successful export depends on information in both the signal peptide and the mature moiety of the protein. To determine the shortest portion of the matu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f10225dea003eeab2e2e4fa440bcf5c
https://doi.org/10.1128/jb.176.11.3397-3399.1994
https://doi.org/10.1128/jb.176.11.3397-3399.1994
Publikováno v:
FEBS letters. 349(2)
Maltose-binding protein (MBP), whose export in E. coli is dependent upon the chaperone SecB, and ribose-binding protein (RBP), whose export is SecB-independent, have been used to generate hybrid secretory proteins. Here, in vitro techniques were used
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32c409fa94ff987943fb00d519d34eb2
https://pubmed.ncbi.nlm.nih.gov/8050582
https://pubmed.ncbi.nlm.nih.gov/8050582
In Escherichia coli, the efficient export of maltose-binding protein (MBP) is dependent on the chaperone SecB, whereas export of ribose-binding protein (RBP) is SecB independent. To localize the regions of MBP involved in interaction with SecB, hybri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bce511a0087e45341ea6505063443fe0
