Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Hedda K. Hoffschulte"'
Autor:
Karl-Ludwig Schimz, Matthias Müller, Juan MacFarlane, Bernd Mechler, Christoph Neumann-Haefelin, Thomas Hengelage, Hedda K. Hoffschulte, Hans-Georg Koch
Publikováno v:
Molecular Biology of the Cell. 10:2163-2173
The molecular requirements for the translocation of secretory proteins across, and the integration of membrane proteins into, the plasma membrane of Escherichia coli were compared. This was achieved in a novel cell-free system from E. coliwhich, by e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::668c09aead7690f43a8134827cadde68
https://doi.org/10.1091/mbc.10.7.2163
https://doi.org/10.1091/mbc.10.7.2163
Autor:
Hedda K. Hoffschulte, Thomas Hengelage, Hans-Georg Koch, Mathias Behrmann, Matthias Müller, Beate Wieseler
Publikováno v:
Journal of Biological Chemistry. 273:13898-13904
An oligodeoxynucleotide-dependent method to generate nascent polypeptide chains was adopted for use in a cell-free translation system prepared from Escherichia coli. In this way, NH2-terminal pOmpA fragments of distinct sizes were synthesized. Becaus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68ca4d497698b5e90716763875a6f023
https://doi.org/10.1074/jbc.273.22.13898
https://doi.org/10.1074/jbc.273.22.13898
Autor:
Ulla E. Swidersky, Annette Rienhöfer-Schweer, Hedda K. Hoffschulte, Friedrich Ernst, Pamela K. Werner, Matthias Müller, Spencer A. Benson
Publikováno v:
European Journal of Biochemistry. 207:803-811
SecY is an integral plasma-membrane protein of Escherichia coli which is essential for the export of periplasmic and outer-membrane proteins containing cleavable signal sequences. We have synthesized SecY in vitro using an E. coli transcription/trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f86d34b1d692f50deee8cc854d3e389d
https://doi.org/10.1111/j.1432-1033.1992.tb17111.x
https://doi.org/10.1111/j.1432-1033.1992.tb17111.x
Publikováno v:
FEMS Microbiology Letters. 91:129-133
The H-subunit of the photosynthetic reaction center of Rhodobacter capsulatus was synthesized in vitro by programming a R. capsulatus cell-free translation system with isolated H-protein mRNA. When intracytoplasmic membrane vehicles of R. capsulatus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e32e5ddad9dff398438fbedacb6d2ed
https://doi.org/10.1111/j.1574-6968.1992.tb05197.x
https://doi.org/10.1111/j.1574-6968.1992.tb05197.x
We have separately analyzed membrane-targeting and membrane translocation of an exported bacterial protein. The precursor of the outer membrane protein LamB of Escherichia coli was synthesized in vitro and translocated into inverted plasma membrane v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74f5d5c56437c422a4b8cb8d5d2d9d14
https://europepmc.org/articles/PMC551882/
https://europepmc.org/articles/PMC551882/
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 661:124-135
Proteinase B (EC 3.4.22.9) was purified from commercial baker's yeast and from wild type strains of Saccharomyces cerevisiae and Saccharomyces carlsbergensis. For large scale purification a procedure was developed involving hydrophobic chromatography
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04b33e42f70df4d04b08d092038b6686
https://doi.org/10.1016/0005-2744(81)90091-7
https://doi.org/10.1016/0005-2744(81)90091-7
Publikováno v:
FEBS Letters. (1):113-116
We have purified to homogeneity a 15 kDa-protein from a ribosomal salt extract of Escherichia coli that compensates in vitro a defect of SecA but not of SecB. Removal of this protein from a cell-free transcription/translation system impairs transloca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78380ae62a6ef34834390ed90a7edcaf
Publikováno v:
Biochimica et biophysica acta. 661(1)
The substrate specificity of proteinase B (EC 3.4.22.9) from Baker's yeast was studied. Experiments with unblocked synthetic peptides indicated that the enzyme has no aminopeptidase activity. The proteinase cleaves trypsin substrates like Bz-Arg-OEt,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30737b3275829a65d015f218cd9b2065
https://pubmed.ncbi.nlm.nih.gov/7028121
https://pubmed.ncbi.nlm.nih.gov/7028121
Publikováno v:
The Journal of Cell Biology
In vitro integration of the polytopic, transmembrane lactose permease into membrane vesicles from Escherichia coli is demonstrated. To this end the enzyme was synthesized in a homologous, cell-free transcription-translation system. In this system, sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95dda16354001c7f1c367fcf80d7d38f
https://pubmed.ncbi.nlm.nih.gov/2654138
https://pubmed.ncbi.nlm.nih.gov/2654138
Publikováno v:
European journal of biochemistry. 181(2)
We demonstrate here the in vitro translocation of yeast acid phosphatase into rough endoplasmic reticulum. The precursor of the repressible acid phosphatase from Saccharomyces cerevisiae encoded by the PHO5 gene, was synthesized in a yeast lysate pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a46bb4b2c9f584d11dfe15ce101262b
https://pubmed.ncbi.nlm.nih.gov/2653826
https://pubmed.ncbi.nlm.nih.gov/2653826