Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protein S5 and S12 were isolated from 30S ribosomal subunits of two E. coli mutants highly resistant to the antibiotic neamine, and of the parental strain. Proteinchemical analyses on these proteins led to the following results: a) In protein S5 the arginine residue in peptide T2 of the parental strain is replaced by glycine in one (nea 314) or serine in the other (nea 319) of the two mutants. b) In protein S12 The proline residue in peptide T15 of the parental strain is replaced by leucine in mutant nea 314 and by glutamine in mutant nea 319. Comparison of these results with those obtained in earlier studies on other mutants with altered ribosomal proteins revealed that the amino acid replacements in neamine resistant mutants and in "revertants" from streptomycin dependence occur at the same amino acid positions of proteins S5 and S12. Therefore it is likely that both types of mutants belong to the same class.
Mol Gen Genet 1975 Dec 23
PMID:Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli. II. Localization of amino acid replacements in proteins S5 and S12 altered in double mutants resistant to neamine. 76 36

The analysis of tryptic peptides was performed on the unassembled as well as assembled form f alpha subunit of the DNA-dependent RNA polymerase from Escherichia coli. The peptide profiles obtained by Dowex 50 column chromatography of the unassembled alpha subunit prepared from cells, either pulse-labeled or continuously labeled with radioactive lysine or arginine, were essentially identical with those of the alpha subunit from intact RNA polymerase. The results suggest that newly synthesized free alpha subunit is assembled into the polymerase structure without any remarkable modifications. The number of lysine- and arginine-containing peaks were close to the values expected from the amino acid composition of alpha subunit assuming that the two alpha subunits in RNA polymerase core enzyme have identical primary structure.
Mol Gen Genet 1976 Jun 15
PMID:Peptide analysis of RNA polymerase alpha subunit from Escherichia coli: comparison of free with assembled form. 78 18

Lambda repressor was purified from an E. coli strain which produces 150 times more lambda repressor than a single lysogen. The sequence of the fifty N-terminal residues was determined by automated Edman degradation. It contains 43% of all arginine and lysine residues of the chain and constitutes according to the genetic data of Oppenheim et al. (1975) a substantial part of the operator-DNA-binding site of the repressor.
Mol Gen Genet 1976 Aug 10
PMID:N-terminal sequence of phage lambda repressor. 78 22

Escherichia coli K12 Hfr H Tsxs Strs and F- Pro- Tsxr His- Arg- Strr bacteria were conjugated in the absence of arginine with or without glucose. The efficiency of conjugation, measured by the frequency of Pro+ and His+ recombinants was not affected. Arginine starvation alone did not affect the tsxs gene expression which occurred in all the zygotes which had received the gene. In contrast, argine and glucose starvation allows tsxs expression only in those zygotes in which the donor gene had been integrated in the genome. As the glucose starvation brings on a destabilization of the messenger RNA synthesized by the F- cells in absence of arginine, the results can be interpreted as follows: the transferred tsxs genes are transitorily expressed in all the zygotes at the unintegrated state. After this transient period, only thsoe genes integrated in the chromosomes of the zygotes continue to be expressed.
Mol Gen Genet 1976 Aug 10
PMID:Effect of glucose starvation on the expression of transferred tsx genes in Escherichia coli K12 zygotes. 78 25

To date, the production of T-even bacteriophage with giant heads has been achieved in two ways: (i) by use of canavanine-arginine treatment of Escherichia coli B cultures infected by wild-type bacteriophage (Cummings and Bolin, Bacteriol. Rev. 40:314-359, 1976; Cummings et al., Virology 54:245-261, 1973), which give a size distribution of giants that is phage specific (Cummings et al., Virology 54:245-261, 1973); and (ii) by infection with certain missense mutants of T4D gene 23 (Doermann et al., J. Virol. 12:374-385, 1973; ICN-UCLA Symposium on Molecular Biology, p. 243-285, 1973) or temperature-sensitive mutants of gene 24 (Aebi et al., J. Supramol. Struct. 2:253-275, 1974; Biljenga et al., J. Mol. Biol. 103:469-498, 1976). We now report the effect of mixed infection with several mutants of T4D on both the production and the size of giant bacteriophage. We found that gene 24 mutant is a critical partner for the production of giants. Infection using T4.24 mutants together with either T4.23 mutants, T4B+ or T6+ led to the formation of giants with heads 10- to 14-fold longer than normal-length heads. Infection with amber 24-bypass 24 double mutants of T4D led to the production of giants when gene 23 mutant was used to co-infect. Addition of canavanine to the co-infected cultures could alter the size distribution of giants, depending on which phage were used to coinfect. Gene 22 mutants had a modifying effect on these results. In the absence of canavanine co-infection with gene 22 mutants prevented the production of giants, and in the presence of canavanine giants of 1.5 to 5 head lengths were found. We have interpreted these results to mean that critical concentrations of gene products 22, 23, and 24 interact to control head length in T-even bacteriophage.
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PMID:Structural aberrations in T-even bacteriophage. IX. Effect of mixed infection on the production of giant bacteriophage. 86 36

1. The effect of intravenous infusion of L-lysine and L-arginine on the tubular reabsorption of dibasic amino acids and cystine was studied in normal individuals and in homozygous and heterozygous subjects with cystinuria. 2. The control subjects reabsorbed almost all filtered lysine and arginine until the filtered load was elevated about fourfold. With further increased loads the tubular reabsorption began to fall and tended to approach a maximum reabsorption rate. By contrast, the homozygous subjects could not reabsorb the elevated amino acid beyond the endogenous capacity until the filtered load was increased seven- to ten-fold. When the filtered load was further increased, tubular reabsorption proceeded at the normal rate in the cystinuric patients. 3. These findings may be explained by a low-capacity transport system, which acts at low substrate concentrations, being defective in the cystinuric subjects, while a high-capacity transport system, which predominates at high substrate concentrations, remains intact. 4. Lysine and arginine infusion depressed the percentage tubular reabsorption of other dibasic amino acids and cystine both in the control and the cystinuric subjects. In the control subjects the amino acid infusion caused a gradual linear fall in the fractional reabsorption of the dibasic amino acids and cystine, whereas the depressed reabsorption of the dibasic amono acids in the cystinuric patients returned to that observed under the endogenous condition when the filtered load was high. The amino acid load caused only a gradual decrease in cystine reabsorption in the cystinuric patients. 5. In the heterozygous subjects the slope of the titration curves and the depression of the tubular reabsorption were intermediate between those of the control and homozygous subjects.
Clin Sci Mol Med 1977 Jul
PMID:Renal handling of dibasic amino acids and cystine in cystinuria. 87 25

Arginine-rich basic protein from cytoplasma of Guerin epitheliomas has been isolated and characterized. It contains five amino acids: arginine, lysine, glycine, alanine and glutamic acid which make together 74% of all amino acid residues. The protein has a cationic character with an isoelectric point of 8.2. No carbohydrate component was found in this protein. The significance of arginine-rich basic protein in the cytoplasma of Guerin epithelioma is discussed briefly.
Mol Cell Biochem 1977 Aug 19
PMID:Characterization of cytoplasmic arginine-rich basic protein of Guerin epithelioma. 90 17

Partially purified D-aspartate oxidase from beef kidney has been tested in the presence of butanedione or phenylglyoxal, which specifically modify the arginine molecule. The results obtained clearly indicate that arginine residues are involved in the binding of the substrate to the active site of the enzyme.
Mol Cell Biochem 1977 Aug 19
PMID:Essential arginine residues in beef kidney D-aspartate oxidase (a preliminary report). 90 20

1. Administration of dexamethasone, 8 mg/day (0-02 mmol/day), for 5 days to normal subjects produced negative nitrogen balance, due to early and sustained increases in urinary urea nitrogen excretion 2. In eight subjects ingesting 0-9--1-6 g of protein day-1 kg-1 body weight the cumulative increment in urea nitrogen excretion averaged + 12-5 g (SEM 2-8, P less than 0-01) over the 5 days of glucocorticoid administration. 3. Increases in urinary urea nitrogen excretion could be related to both plasma alanine and blood glutamine changes by using a multiple regression equation. 4. These results suggest that corticosteroids induce increased release of alanine and glutamine by peripheral tissues, which may augment urea formation and negative nitrogen balance. 5. The correlation between increments in urea nitrogen excretion and increases in plasma arginine remains unexplained.
Clin Sci Mol Med 1977 Sep
PMID:The role of alanine and glutamine in steroid-induced nitrogen wasting in man. 91 44

The A-protein of coliphage MS2 was purified to a state of sufficient homogeneity to study its primary structure. The NH2-terminal sequence was determined for the first 8 residues. Comparison with the reported sequence of R17 protein (Weiner, A. M., Platt, T., and Weber, K. (1972) J. Biol. Chem. 247, 3242-3251) shows a difference at position 6 where alanine in R17 is replaced by threonine in MS2. The COOH-terminal sequence was shown to be -Arg-Leu-Ser-Arg, confirming the existence of UAG as the termination codon of the maturation protein (Comtreras, R., Ysebaert, M., Min Jou, W., and Fiers, W. (19731 Nature New Biol. 241, 99-101; Vandekerckhove, J., Nolf, F., and Van Montagu, M. C. (1973) Nature New Biol. 241, 102; Remaut E., and Fiers, W. (1972) J. Mol. Biol. 71, 243-261). Peptides obtained by enzymatic hydrolysis with trypsin were fractionated by a combination of gel filtration and paper electrophoresis and chromatography. Thirty-eight peptides were analyzed for amino acid composition and sequence. They provide information for 312 of the 393 residues of the A-protein polypeptide chain.
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PMID:Sequence of the A-protein of coliphage MS2. I. Isolation of A-protein, determination of the NH2- and COOH-terminal sequences, isolation and amino acid sequence of the tryptic peptides. 91 36


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