Výsledky vyhledávání - "R L, Somerville"

Synechocystis PCC 6803 contains a single gene for the beta subunit of tryptophan synthase with strong homology to the trpB genes of Arabidopsis and maize (Zea mays L.)

Autor: P. R. Chitnis, Guo-Ping Zhao, R. L. Somerville

Publikováno v: Plant physiology. 104(2)

We report the sequence of the trpB gene of the cyanobacterium Synechocystis sp. PCC 6803. This gene was cloned from a plasmid library by functional complementation of a trpB mutant of Escherichia coli K-12. Among the known trpB sequences, the Synecho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4479c1a8f139ac8de628b0bdd767fc2c
https://pubmed.ncbi.nlm.nih.gov/8159786

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An amino acid switch (Gly281--Arg) within the 'hinge' region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody

Autor: G P, Zhao, R L, Somerville

Publikováno v: The Journal of biological chemistry. 268(20)

The in vitro susceptibility to endogenous proteases of the beta subunit of Escherichia coli tryptophan synthase was studied immunochemically. Whereas the wild-type beta subunit was apparently very stable, the missense mutant beta(B8), carrying an ami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5bdc4fcde807f1a8db9290e50da781a
https://pubmed.ncbi.nlm.nih.gov/8325868

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A single amino acid switch within the 'hinge' region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product

Autor: G P, Zhao, R L, Somerville

Publikováno v: The Journal of biological chemistry. 268(20)

The trpB8 mutation of Escherichia coli causes a major conformational change within the beta subunit of tryptophan synthase. The basis of this effect is a replacement of glycine 281 by arginine within a structurally important "hinge" region. The mutan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4177929c72c514be0e4167197af17238
https://pubmed.ncbi.nlm.nih.gov/8325869

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The TyrR protein of Escherichia coli, analysis by limited proteolysis of domain structure and ligand-mediated conformational changes

Autor: J, Cui, R L, Somerville

Publikováno v: The Journal of biological chemistry. 268(7)

The TyrR protein of Escherichia coli K12 is a homodimer containing 513 amino acids/subunit. This protein is important in the transcriptional regulation of several genes whose protein products catalyze steps in aromatic amino acid biosynthesis or tran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f276b395b1675937ab8a4620e9e4a8d4
https://pubmed.ncbi.nlm.nih.gov/8444880

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Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive 'hinge' region diminishes substrate binding and alters solubility

Autor: G P, Zhao, R L, Somerville

Publikováno v: The Journal of biological chemistry. 267(1)

The trpB8 mutation of Escherichia coli tryptophan synthase is unique in that the cells bearing this lesion are not only capable of utilizing indole for growth, but they also accumulate indole, under conditions of tryptophan limitation. The lesion was

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d77e836931b51a3548002bf3788b0a46
https://pubmed.ncbi.nlm.nih.gov/1309752

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A human hepatocellular carcinoma 3.0-kilobase DNA sequence transforms both rat liver cells and NIH3T3 fibroblasts and encodes a 52-kilodalton protein

Autor: S S, Yang, K, Zhang, W, Viera, J V, Taub, J H, Zeilstra-Ryalls, R L, Somerville

Publikováno v: Cancer research. 50

Neoplastic transformation of rat liver cells in vitro by DNA-mediated gene transfer with an oncogene, hhcM, derived from human (Mahlavu) hepatocellular carcinoma, is described and compared with that of NIH3T3 cells. hhcM was cloned in a neomycin-resi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c266058e44c97a905cbd25ef949680c7
https://pubmed.ncbi.nlm.nih.gov/2167164

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Evidence that repression mechanisms can exert control over the thr, leu, and ilv operons of Escherichia coli K-12

Autor: D I Johnson, R L Somerville

Publikováno v: Journal of Bacteriology. 155:49-55

Mutants of Escherichia coli K-12 resistant to either the threonine analog DL-alpha-amino-beta-hydroxyvaleric acid or the leucine analog 5',5',5'-trifluoro-DL-leucine were isolated. One DL-alpha-amino-beta-hydroxyvaleric acid-resistant mutant strain,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bac567aa090a0de9107f0a25a7bbf12b
https://doi.org/10.1128/jb.155.1.49-55.1983

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