Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Ronald L. Somerville"'
Publikováno v:
Journal of Bacteriology. 182:1053-1061
The TyrR protein of Escherichia coli (513 amino acid residues) is the chief transcriptional regulator of a group of genes that are essential for aromatic amino acid biosynthesis and transport. The TyrR protein can function either as a repressor or as
Autor:
Ronald L. Somerville, Weiping Yang
Publikováno v:
Methods. 19:322-329
Anti-idiotypic antibodies were obtained from New Zealand White rabbits injected with affinity-purified rabbit anti-TrpR antibodies. In gel mobility shift studies, such immunoglobulin preparations were shown to contain one or more species able to form
Autor:
Ronald L. Somerville, Shimin Zhao
Publikováno v:
Journal of Biological Chemistry. 274:1842-1847
Highly purified preparations of the TyrR protein of Haemophilus influenzae Rd undergo specific and limited proteolytic cleavage during storage at 4 degreesC to generate two fragments of 28 and 8 kDa. Under nondenaturing conditions, the two fragments
Autor:
Qing Bai, Ronald L. Somerville
Publikováno v:
Journal of Bacteriology. 180:6173-6186
Autor:
Ronald L. Somerville, Hong Qiu Smith
Publikováno v:
Journal of Bacteriology. 179:5914-5921
The ability of microorganisms to degrade L-tyrosine to phenol, pyruvate, and ammonia is catalyzed by the inducible enzyme L-tyrosine phenol lyase (EC 4.1.99.2). To investigate possible mechanisms for how the synthesis of this enzyme is regulated, a v
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1253:208-214
The oxidation of L-threonine to 2-amino-ketobutyrate, as catalyzed by L-threonine dehydrogenase, is the first step in the major pathway for threonine catabolism in both eukaryotes and prokaryotes. Threonine dehydrogenase of E. coli has considerable a
Autor:
Ihor Skrypka, Ronald L. Somerville
Publikováno v:
DNA Sequence. 4:355-360
The sequence of the Salmonella typhimurium trpR gene and flanking DNA was determined on both strands. The DNA sequence predicts a polypeptide product of 108 amino acids with a molecular weight of 12,274 daltons. The TrpR protein of S. typhimurium dif
Autor:
Ronald L. Somerville, Guo-Ping Zhao
Publikováno v:
Journal of Biological Chemistry. 268:14921-14931
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
Autor:
Ronald L. Somerville, Guo-Ping Zhao
Publikováno v:
Journal of Biological Chemistry. 268:14912-14920
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
Publikováno v:
Proceedings of the National Academy of Sciences. 90:5796-5800
Highly purified preparations of trp repressor (TrpR) protein derived from Escherichia coli strains that were engineered to overexpress this material were found to contain another protein, of 21 kDa. The second protein, designated WrbA [for tryptophan