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Query: UNIPROT:P06889 (
Mol
)
630,302
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Selection for defective reversion induction, after UV treatment of E. coli
K 12
, yielded uvm mutants. These mutants exhibited highly reduced or no UV mutability for all loci tested although they were moderately and normally mutable by X-rays and EMS, respectively. Uvm mutations confer only a slight sensitivity to killing by UV and X-rays and no clear sensitivity to the lethal effect of HN2, EMS or MMS. Growth and viability of untreated uvm cells were normal. The properties of uvm mutants are discussed in relation to those of other relevant mutant types and to some actual problems of induced mutagenesis.
Mol
Gen Genet 1978 Sep 20
PMID:Uvm mutants of Escherichia coli K12 deficient in UV mutagenesis. I. Isolation of uvm mutants and their phenotypical characterization in DNA repair and mutagenesis. 36 69
Polar mutations were obtained by integration of bacteriophage Mu c+ or Mu cts DNA into the Klebsiella pneumoniae nif genes located on plasmid pCE1, a derivative of pRD1. In addition, nif deletions were isolated from nif::Mu cts plasmids. Complementation data allowed the characterization of twelve nif cistrons, nine corresponding to previously identified genes. Polar effect of Mu DNA insertions suggested the existence of at least six transcription units: 1) nif K, nif D and nif H--2)nif A and nif L--3) nif E and a new gene--4) nif B--5) nif F--6) nif J. Nif K, nif D and nif H, which are most probably the structural genes for nitrogenase, seem to belong to the same operon transcribed from nif H to nif K. This was confirmed by
SDS
gel autoradiography of pulse labelled proteins. Moreover it was possible to identify, on the autoradiograms, a polypeptide which likely is the product of nif J and whose biosynthesis is under the control of nif A.
Mol
Gen Genet 1978 Oct 04
PMID:Genetic and biochemical analysis of mutants induced by bacteriophage Mu DNA integration into Klebsiella pneumoniae nitrogen fixation genes. 36 77
SDS
-polyacrylamide gel analysis of P22-infected Salmonella has allowed identification of the c2 repressor (MW 31,000) and study of repressor synthesis in regulatory mutants of P22. Repressor is synthesized in reduced amounts or is absent in infections with P22, clNo.7, P22, c2 am08, P22 c3 am03, and P22 c3 am012, but is synthesized in markedly increased amounts in the virulent mutant, P22 virB3, and its component mutants, vx and k5. Higher levels of repressor are also found in the P22 cly 17 mutant.
Mol
Gen Genet 1979 Jan 02
PMID:Repressor synthesis in regulatory mutants of bacteriophage P22. 36 97
Streptomycin-independent revertants were selected from streptomycin-dependent mutants. Twenty-five out of 150 such revertants were temperature sensitive. Ribosomal proteins from 18 temperature-sensitive and 10 temperature-insensitive revertants were analysed by
SDS
-polyacrylamide gel electrophoresis. Seventeen of the former but none of the latter category showed an alteration of protein S4. The mutated rpsD allele of 6 temperature-sensitive revertants was transduced into a rpsL+ strain. In all cases an increased suppressibility of T4 amber phages was observed. Such suppressibility was not observed in the original rpsD, rpsL strains. All 18 temperature-sensitive mutants were disturbed in the processing of 17s to 16s RNA at non-permissive temperature and the accumulated 17s RNA was degraded. Temperature-insensitive rpsD revertants could be isolated, which had gained a second alteration in S4. Such revertants, which had lost the temperature-sensitive property, were also unable to suppress growth of T4 amber phages. It is concluded that temperature-sensitive growth, inability to process 17s RNA and to assemble 30S ribosomes at non-permissive temperature as well as increased translational ambiguity are highly correlated properties in rpsD mutants.
Mol
Gen Genet 1979 Feb 01
PMID:Analysis of rpsD mutations in Escherichia coli. I. Comparison of mutants with various alterations in ribosomal protein S4. 37 47
A set of lambda transducing phages carrying varying lengths of the E. coli chromosome around the structural gene for initiation factor IF3 (infC) was derived from lambda p2 which is known to carry, besides infC, the structural genes for the alpha subunit of phenylalanyl-tRNA synthetase (pheS), the beta subunit of phenylalanyl-tRNA synthetase (pheT) and the structural gene for threonyl-tRNA synthetase (thrS). The E. coli coding content of these derived phages was analysed by genetic complementation of a set of mutants and by
SDS
-polyacrylamide gel analysis of the proteins synthesized in UV irradiated cells infected with these phages. The segregation pattern of the different genes among these derived phages indicates that the order of the genes is pheT - pheS - "P12" - (infC, thrS) where infC is probably between "P12" and thrS. "P12" is the structural gene of a 12,000 molecular weight unidentified protein.
Mol
Gen Genet 1979 Feb 01
PMID:Genetic organization of the E. coli chromosome around the structural gene for initiation factor IF3 (infC). 37 55
The composition of structural proteins of lambdoid phages such as lambda, phi 80 434 divided by molecular weights was determined by means of
SDS
-disc-electrophoresis in a 15% polyacrylamide gel. The proteins of the same phages were divided by isoelectric points using an isoelectric focusing in a 5,25% polyacrylamide gel with 8 M urea and a gradient pH 7.0--3.5. The both methods brought out a composition character of the virion proteins and illustrated the high degree of similarity among the structural proteins of phages lambda and 434 and a far less similarity among the proteins lambda and phi 80. The antigenic composition of the lambdoid phage was determined and the basic antigenes were identified on one-dimensional and two-dimensional immunoelectrophoregrams. The appreciable immunochemical affinity of basic antigenes of the lambda and 434, but a partial affinity of the phages lambda and phi 80 were found. The basic protein of the head pE proved to be immunochemically similar for all three phages.
Mol
Biol (Mosk)
PMID:[Lambdoid phage structural proteins and antigens]. 37 13
The E. coli dnaK (groPC756) gene product is essential for bacteriophage lambda DNA replication. Bacterial DNA segments carrying this gene have been cloned onto a bacteriophage lambda vector. The product of the dnaK gene has been identified on
SDS
polyacrylamide gels after infection of UV-irradiated E. coli cells. The dnaK gene codes for a polypeptide with an apparent molecular weight of 93,000-Mr. Transducing phages carrying amber mutations in the dnaK gene fail to induce the synthesis of the 93,000-Mr polypeptide chain upon infection of sup+ bacteria, but do so upon infection of supF bacteria. E coli carrying the dnaK756 mutation are, in addition, temperature sensitive for growth at 43 degrees C. It is shown that the dnaK756 mutation results in an overproduction of the dnaK gene product at that temperature.
Mol
Gen Genet 1979 May 04
PMID:Identification of the C. coli dnaK (groPC756) gene product. 38 43
Several E. coli mutants were isolated which produce triple chimeras between one of the trp enzymes lac, repressor and beta-galactosidase. The mutants were isolated as TonB- Lac+ derivatives of a phenotypically Lac- TrpR- strain carrying a lac I+ -Z+ fusion on a phi80dlac phage. The phage is integrated into the chromosome in such a way that the lac and the trp genes are transcribed in the same direction. Of a total of 58 candidates 2 TrpA- and 3 Trp- strains produce triple chimeras. The chimeras from the two TrpA- strians were further examined. They consist of tryptophan synthetase alpha-subunit, lac repressor and beta-galactosidase. In crude extracts of these strains the tryptophan synthetase alpha-subunit part can be identified by its ability to aggregate with the beta-subunit since some of the beta-subunit activity can be precipitated with antiserum against beta-galactosidase. Furthermore beta-galactosidase precipitates with antiserum against tryptophan synthetase alpha-subunit. The lac repressor part is able to bind IPTG, but not lac operator DNA in vitro. The beta-galactosidase part is as unaffected as in the original lac repressor-beta-galactosidase chimera. The molecular weights of both chimeras are 175,000 when determined by
SDS
gel electrophoresis. The chimeras are partially degraded giving rise to fragments of distinct molecular weights.
Mol
Gen Genet 1977 Oct 24
PMID:Synthetic multifunctional proteins: isolation of covalently linked tryptophan synthetase alpha-subunit-lac-repressor-beta-galactosidase chimeras. 41 64
A DNA protein complex has been isolated from vegetative cells and spores of Bacillus subtilis. Properties of the DNA protein complex prepared from vegetative cells were studied and
SDS
gel electrophoresis was employed to compare the different DNase-untreated and -treated DNA protein complexes. It is concluded that proteins are associated with the DNA and differences in protein pattern in polyacrylamide gels indicates the involvement of DNA-binding proteins in the regulation of spore formation.
Mol
Gen Genet 1978 Feb 16
PMID:Differences in pattern of a DNA protein complex isolated from vegetative cells and spores of Bacillus subtilis. 41 35
Conditions for the isolation of intact poly(A)+mRNP from cryptobiotic gastruale of A. salina are described. In the presence of Mg2+ ions nucleolytic cleavage occurs in vitro in the vicinity of the 3'-poly(A) segment of mRNP during the isolation procedure. The resulting two parts of poly(A)+mRNP complex are separated by thermal elution from oligo(dT)-cellulsoe affinity column. Analysis by
SDS
-gel electrophoresis of protein components associated with intact poly(A)+mRNP has revealed the existence of 20--30 S RNP complex containing five major proteins with Mr 68,000, 53,000, 50,000, 45,000 and 38,000, respectively, but completely lacking the poly(A)-specific Mr 76,000 protein.
Mol
Biol Rep 1979 May 31
PMID:Characterization of protein components of poly(A)-containing messenger ribonucleoproteins from cryptobiotic gastrulae of Artemia salina. 46 Jan 83
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