Výsledky vyhledávání - "L L, Randall"

Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export

Publikováno v: Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 339:343-354

SecB is a molecular chaperone involved in protein export from Escherichia coli . It is a highly negatively charged, soluble, tetrameric protein with a monomer molecular mass of 16 400 kDa. It has two functions: it maintains precursors of some exporte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae36c8834eabebc48701e66ced49c4bf
https://doi.org/10.1098/rstb.1993.0033

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SecB, one small chaperone in the complex milieu of the cell

Autor: S. J. S. Hardy, L. L. Randall

Publikováno v: Cellular and molecular life sciences : CMLS. 59(10)

SecB is only one of a plethora of cytosolic chaperones in E. coli whose common property is that they bind nonnative proteins. It plays a crucial role during protein export via the general secretory pathway by modulating the partitioning of precursors

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28e333d2d89c733f1895c7c5ff9e4423
https://pubmed.ncbi.nlm.nih.gov/12475171

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Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions

Autor: R L, Woodbury, T B, Topping, D L, Diamond, D, Suciu, C A, Kumamoto, S J, Hardy, L L, Randall

Publikováno v: The Journal of biological chemistry. 275(31)

During localization to the periplasmic space or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted to the membrane by specific interaction with SecA, a periphera

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9621df498ef90d7a8414df92a4ca39bc
https://pubmed.ncbi.nlm.nih.gov/10807917

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SecB: a chaperone from Escherichia coli

Autor: L L, Randall, T B, Topping, V F, Smith, D L, Diamond, S J, Hardy

Publikováno v: Methods in enzymology. 290

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ab9a1a93be74cb1547583e34f8b30ab0
https://pubmed.ncbi.nlm.nih.gov/9534181

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Kinetic partitioning. Poising SecB to favor association with a rapidly folding ligand

Autor: D L, Diamond, L L, Randall

Publikováno v: The Journal of biological chemistry. 272(46)

Chaperones are a class of proteins that possess the remarkable ability to selectively bind polypeptides that are in a nonnative state. The selectivity of SecB, a molecular chaperone in Escherichia coli, for its ligands can be explained in part by a k

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3d0ec33740cfa23737cda0d06715cfd
https://pubmed.ncbi.nlm.nih.gov/9360972

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Electrospray mass spectrometric investigation of the chaperone SecB

Autor: V F, Smith, B L, Schwartz, L L, Randall, R D, Smith

Publikováno v: Protein science : a publication of the Protein Society. 5(3)

Electrospray ionization mass spectrometry was used to investigate the structure of the Escherichia coli chaperone protein SecB. It was determined that the N-terminal methionine of SecB has been removed and that more than half of all SecB monomers are

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c90b2076f20e4d7bbd94501d4d8ca76f
https://pubmed.ncbi.nlm.nih.gov/8868485

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Interaction of SecB with intermediates along the folding pathway of maltose-binding protein

Autor: D L, Diamond, S, Strobel, S Y, Chun, L L, Randall

Publikováno v: Protein science : a publication of the Protein Society. 4(6)

SecB, a molecular chaperone involved in protein export in Escherichia coli, displays the remarkable ability to selectively bind many different polypeptide ligands whose only common feature is that of being nonnative. The selectivity is explained in p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a23b77158dc983c76c5d1fae0785aa88
https://pubmed.ncbi.nlm.nih.gov/7549876

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Determination of the binding frame within a physiological ligand for the chaperone SecB

Autor: T B, Topping, L L, Randall

Publikováno v: Protein science : a publication of the Protein Society. 3(5)

The hallmark of the class of proteins called chaperones is the amazing ability to bind tightly to a wide array of polypeptide ligands that have no consensus in sequence; chaperones recognize non-native structure. As a step in the elucidation of the m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5963cd9f7087cc525cf4f9fc79deb646
https://pubmed.ncbi.nlm.nih.gov/8061603

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Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro

Autor: S Y, Chun, S, Strobel, P, Bassford, L L, Randall

Publikováno v: The Journal of biological chemistry. 268(28)

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=pmid________::326292bb66779e1b0c90f8ab696c9aeb
https://pubmed.ncbi.nlm.nih.gov/8407916

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