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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

The F34 mutant strain of Chlamydomonas reinhartii is deficient in photosystem II reaction centers. The E fracture faces of the thylakoid membranes of this mutant show a considerable reduction in the number of particles present ant in their size compared with the wild type. We conclude that the polypeptides associated with photosystem II reaction centers, which are missing in SDS polyacrylamide gel electrophoresis patterns of proteins from this mutant strain, are part of the EF particles and are required for assembly of these particles.
Mol Biol Rep 1979 Aug 31
PMID:Ultrastructure - function relationship in Chlamydomonas reinhartii thylakoids, by means of a comparison between the wild type and the F34 mutant which lacks the photosystem II reaction center. 49 57

Purified rat liver nuclei were incubated at 4 degrees C. After different intervals of incubation aliquots of the nuclear suspension were taken and DNA was extracted by a common SDS-phenol-chloroform procedure. The fractionation of DNA by agar gel electrophoresis revealed large DNA fragments. It was shown that the well-known DNA degradation to monomers and its multiples is preceeded by an earlier breakdown of DNA into characteristic large fragments.
Mol Biol Rep 1979 Aug 31
PMID:DNA degradation in isolated rat liver nuclei. 49 62

We describe here a fluorometric method of detection of proteins fractionated by electrophoresis in polyacrylamide-SDS gels. This method, using ethidium bromide as fluorescent dye, is performed within 40 minutes after the end of the electrophoretic run. It does not require treatment of proteins prior to electrophoresis, and entails neither fixation of proteins in the gel, nor destaining. It is sufficiently sensitive to detect 0.5 - 1.0 microgram of protein per band. Furthermore, the simultaneous electrophoretic resolution and detection of protein and RNA on a single SDS-polyacrylamide gradient gel is reported.
Mol Biol Rep 1979 Dec 31
PMID:A rapid and sensitive method for detection of proteins in polyacrylamide SDS gels: staining with ethidium bromide. 53 Feb 69

Rough endoplasmic reticulum membranes were dissolved in 1% deoxycholate and the deoxycholate was then dialysed out for five days. Well-defined bilayer vesicles were formed only if the dialysis was performed at room temperature for the first six hours. The vesicles were separated into a pelleted fraction (Fraction 1) and a fluffy layer (Fraction II) by centrifugation. As measured by amino acid incorporation ability, Fraction II bound polysomes, while Fraction I did not. When smooth endoplasmic reticulum was assembled, it was found that Fraction II so derived had a polysome binding capacity which was more sensitive to increased KCl concentrations (25 mM - 100 mM KCl) and that it bound significantly more monosomes than the corresponding fraction derived from rough membranes. The SDS-polyacrylamide polypeptide patterns of the various fractions were compared.
Mol Biol Rep 1978 Jun 16
PMID:The in vitro reassembly of rough endoplasmic reticulum: ribosome binding capacity. 68 83


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