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At least 307 records · Page 17Linked to original sources
PubMed1995

A novel amber mutation in a beta zero-thalassaemia gene (beta 37TGG-->TAG), with direct detection by mapping the restriction fragments in amplified genomic DNA.

A novel amber mutation, a G to A substitution at the second position of codon 37 in the beta-globin gene that changes the tryptophan coding triplet (TGG) to a termination codon (TAG), was found in a Chinese beta-thalassaemia carrier. The mutant gene creates an additional Dde I recognition site and eliminates the Ava II site, so this point mutation can be directly identified by restriction enzyme analysis.

Adult↗
PubMed1989

Genes for biosynthesis and assembly of CS3 pili of CFA/II enterotoxigenic Escherichia coli: novel regulation of pilus production by bypassing an amber codon.

The complete nucleotide sequence of the 4746bp HindIII fragment encoding the genes for the biosynthesis and assembly of CS3 pili has been determined. By site-directed mutagenesis in conjunction with analysis of the plasmid-encoded proteins in minicells, the actual reading frames for the various products have been determined. This demonstrated that the genes for four of the proteins (63 kD, 48 kD, 33 kD, and 20 kD in size) are encoded entirely within the same open reading frame as a fifth protein (104 kD). However, for synthesis of this latter protein, suppression or readthrough of an internal amber codon is required. Termination at this codon is also necessary for synthesis of the former proteins. Two further proteins are also encoded within the HindIII fragment: a 27 kD precursor of a periplasmic protein and the 17.5kD precursor of the major CS3 fimbrial subunit.

Amino Acid Sequence↗
PubMed1989

Characterization of amber mutations in bacteriophage Mu transposase: a functional analysis of the protein.

We have characterized a series of amber mutations in the A gene of bacteriophage Mu encoding the phage transposase. We tested different activities of these mutant proteins either in a sup0 strain or in different sup bacteria. In conjunction with the results described in the accompanying paper by Bétermier et al. (1989) we find that the C-terminus of the protein is not absolutely essential for global transposase function, but is essential for phage growth. Specific binding to Mu ends is defined by a more central domain. Our results also reinforce the previous findings (Bétermier et al., 1987) that more than one protein may be specified by the A gene.

Amino Acid Sequence↗
PubMed1980

Polyamines stimulate suppression of amber termination codons in vitro by normal tRNAs.

Polyamines, such as spermine and spermidine, are able to stimulate reading of amber termination codons on viral messenger RNAs in vitro. This phenomenon is not due to an overall increase of error frequency during translation, but to a specific effect on a normal tRNA that is present in various eukaryotic cell preparations. The enhancement of reading of termination codons by normal tRNAs should be of major importance for the expression of specific genes in eukaryotic cells.

Animals↗
PubMed1988

Assembly of amber fragments of the beta subunit of Escherichia coli RNA polymerase.

Immunoblotting of size-separated whole cell proteins permitted the study of protein-protein interaction. Briefly, proteins obtained from cleared cell lysates of Escherichia coli were separated by glycerol gradient centrifugation and analysed by blotting against a set of specific antibodies. We have applied this procedure to the assembly of 11 N-terminal amber fragments of the beta subunit of E. coli RNA polymerase ranging in size between 97% and 23% the length of the intact beta polypeptide (1342 amino acids). In this way, we have been able to define regions on the beta polypeptide involved in the assembly of RNA polymerase.

Centrifugation, Density Gradient↗
PubMed1992

DNA sequences from a fossil termite in Oligo-Miocene amber and their phylogenetic implications.

DNA was extracted from the fossil termite Mastotermes electrodominicus preserved in Oligo-Miocene amber (25 million to 30 million years old). Fragments of mitochondrial [16S ribosomal DNA (rDNA)] and nuclear (18S rDNA) genes were amplified by polymerase chain reaction. Phylogenetic analysis of fossil and extant 18S rDNA confirmed morphological cladistic analyses of living dictyopterans (termites, cockroaches, and mantids). The fossil termite shares several sequence attributes with Mastotermes darwiniensis. Addition of this fossil to living-species phylogeny is required to substantiate Mastotermes monophyly and affects molecular phylogenetic hypotheses of termites in this, the oldest DNA yet characterized.

Animals↗
PubMed1970

Genetic mapping and dominance of the amber suppressor, Su1 (supD), in Escherichia coli K-12.

In this report Su1 (supD), which is known to suppress "amber" mutations by means of a specific transfer ribonucleic acid, has been mapped relative to his and uvrC and has been found to be located at about 37.5 min on the Taylor and Trotter genetic map of the Escherichia coli K-12 chromosome. In addition, Su1(+) has been shown to be dominant over Su1(-), which supports the idea that Su1 is the structural gene for the suppressing transfer ribonucleic acid.

Alkaline Phosphatase↗
PubMed1974

Proteins of the inner membrane of Escherichia coli: changes in composition associated with anaerobic growth and fumarate reductase amber mutation.

The inner membrane fractions of Escherichia coli grown anaerobically and aerobically were isolated, and their proteins were compared by electrophoresis in polyacrylamide gels. To maximimize the differences between the preparations, the anaerobic cultures were grown on complex medium with added glucose, but glucose was omitted from the aerobic cultures to prevent catabolite repression. The pattern of bands in the two types of preparation differed considerably, and changes in approximately 20 components were observed. In particular, the band identified as succinate dehydrogenase in aerobic preparations was greatly reduced in anaerobic preparations. Mutants lacking fumarate reductase were isolated, and inner membrane preparations of an frd amber mutant were deficient in a major component of 75,000 daltons and possibly a minor one of 87,500 daltons. The former was also present in greater amounts in anaerobic preparations and could represent a fumarate reductase subunit.

Aerobiosis↗
PubMed1975

Isolation and characterization of lambda transducing bacteriophages for the su1+ (supD minus) amber suppressor of Escherichia coli.

Specialized lambda transducing phages for the sul+ (supD-) amber suppressor in Escherichia coli K-12 have been isolated, using a secondary site lambda-cI857 lysogen in which we have shown the prophage to be closely linked to sul+.sul+ transducing particles were detected frequently, at 10-5 per plaque-forming unit, in lysates prepared from the secondary-site lysogens. High-frequency transducing lysates were obtained from several independently isolated sul+ transductants and were analyzed by CsCl equilibrium density gradient centrifugation. The transducing phages are defective; marker rescue analysis indicates that the lambda-N gene is not present. In lambda-cI857DELTANdSul+, a bio-type transducing phage, the genes specifying recombination and excision functions have been replaced by bacterial deoxyribonucleic acid.

Centrifugation, Density Gradient↗
PubMed1980

Polarity of amber mutations in ribosomal protein genes of Escherichia coli.

Two amber mutations have been mapped inside the spcA-strA region (now called rpsE-rpsL) on the bacterial genome. Derivatives of the transducing phage lambda fus3 carrying each mutation were constructed and assayed in ultraviolet-irradiated bacteria to identify the mutated genes and measure the polarity of the mutations. The data indicated that both mutations, 3162(Am) and 3161(Am), affect genes coding for ribosomal proteins: rplC (L3) and rpsN (S14), respectively. It was shown also that each mutation exerts, inside of its respective operon (S10 and spc units), a relatively strong polar effect on genes distal to the mutated locus.

Bacterial Proteins↗
PubMed1980

Amber mutation affecting the length of Escherichia coli cells.

An amber mutation in a newly found gene (wee) of Escherichia coli has been isolated from strain OV-2, which harbors a temperature-sensitive suppressor. At 42 degrees C cells of the mutant, OV-25, increased in mass and deoxyribonucleic acid content and divided at normal rates, compared with the wild type under the same growth conditions. Total cell length increased under the restrictive conditions, although at a slightly lower rate. Values of mean cell length and cell volume, contrary to what would be expected from the increment in the rate of increase in particles, mass, and deoxyribonucleic acid, became at 42 degrees C smaller than those found in the wild type. A parallel increase in protein content per length and cell density and a loss of viability were found to occur after four generations at the restrictive temperature. The behavior of strain OV-25 in the absence of the wee gene product could be interpreted in terms of either a faulty regulation of the elongation processes or their abnormal coordination with the cell cycle. The genetic location of the wee gene has been found to be at 83.5 min on the E. coli genetic map.

Cell Division↗
PubMed1981

High-efficiency, temperature-sensitive suppression of amber mutations in Escherichia coli.

We have constructed a high-copy-number plasmid carrying an allele of the supD gene (supD43,74). The plasmid conferred temperature-sensitive suppression of amber mutations. Strains carrying the plasmid exhibited 50 to 60% suppression at 30 degrees C but little or no suppression at 42 degrees C. After a temperature shift from 30 to 42 degrees C the efficiency of suppression decreased gradually over a 60- to 90-min period before reaching the 42 degrees C steady-state level of suppression.

Escherichia coli↗
PubMed1981

An amber mutation in a ribosomal protein gene: ineffective suppression stimulates operon-specific transcription.

The effects of inefficient suppression and the accompanying polarity of an amber mutation in the ribosomal protein gene rplC (L3) on the transcriptional activities of several ribosomal protein operons were investigated. The L3 gene is proximally located in the S10 operon. Inefficient suppression of the mutation specifically stimulated transcription of regions both proximal and distal to the site of mutation by about twofold. In contrast, no effect on the transcriptional activity of regions within the alpha and spc ribosomal protein operons was observed. Thus, transcription of the S10 operon could be actively and specifically regulated in response to a deficiency in one or more of the protein products from the operon. We presume that this transcriptional control acts at the level of transcription initiation, but we cannot exclude the possibility of some other unknown transcriptional regulatory mechanism.

Bacterial Proteins↗
PubMed1991

Temperature sensitivity caused by missense suppressor supH and amber suppressor supP in Escherichia coli.

The temperature-sensitive missense suppressor supH and amber suppressor supP in Escherichia coli are mutations of the serU and leuX genes, respectively. The supH tRNA, tRNA(SerCAA), is expected to recognize UUG codons, which are normally read by tRNA(LeuCAA) and tRNA(LeuUAA), coded for by the leuX gene and the leuZ gene, respectively. We show that supP and supH are incompatible and that strains carrying both supP and a restrictive rpsL allele are temperature sensitive. It is suggested that the temperature sensitivity of both supH and supP strains is caused by deficient reading of UUG codons by tRNA(LeuUAA).

Base Sequence↗
PubMed1992

Amino acid substitution in the lactose carrier protein with the use of amber suppressors.

Five lacY mutants with amber stop codons at known positions were each placed into 12 different suppressor strains. The 60 amino acid substitutions obtained in this manner were tested for growth on lactose-minimal medium plates and for transport of lactose, melibiose, and thiomethylgalactoside. Most of the amino acid substitutions in the regions of the putative loops (between transmembrane alpha helices) resulted in a reasonable growth rate on lactose with moderate-to-good transport activity. In one strain (glycine substituted for Trp-10), abnormal sugar recognition was found. The substitution of proline for Trp-33 (in the region of the first alpha helix) showed no activity, while four additional substitutions (lysine, leucine, cysteine, and glutamic acid) showed low activity. Altered sugar specificity was observed when Trp-33 was replaced by serine, glutamine, tyrosine, alanine, histidine, or phenylalanine. It is concluded that Trp-33 may be involved directly or indirectly in sugar recognition.

Amino Acid Sequence↗