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)

Using purified yeast mitochondrial DNA as a template for E. coli RNA polymerase (holoenzyme) complementary mitochondrial RNA has been synthesized in vitro. This RNA has been used to direct a low background E. coli S-30 protein-synthesizing system. The synthesis of mitochondrial polypeptides has been detected by using antiserum raised against purified cytochrome c oxidase holoenzyme and shown to be specific for this antigen. The antiserum-antigen complex was dissociated and subject to SDS-polyacrylamide gel electrophoresis and the presence of 3 polypeptides of 39, 31, and 26 X 10(3) daltons molecular weight demonstrated, which correspond to the subunits synthesized by mitochondria in whole cells which are inhibited with cycloheximide.
Mol Gen Genet 1977 Jan 07
PMID:Synthesis of cytochrome c oxidase polypeptides in an Escherichia coli cell-free system directed by Saccharomyces cerevisiae mitochondrial DNA. 18 80

Particles carrying heterogeneous nuclear RNA (30 S-particles) were prepared from rat liver and Zajdela hepatoma ascites cell nuclei after ultrasonic disruption. The ribonucleoprotein structures were disintegrated in the presence of 100mM spermidine. Using chromatography on Sepharose-polyadenylate a protein component has been obtained which possessed high affinity for heterogeneous nuclear RNA, polyuridylate and polyadenylate, and double-stranded DNA. This protein was the main species of the ribonucleoprotein studied; it showed bands with molcular weights of 37000 and 40000 respectively in SDS gel electrophoresis. The RNA-binding proteins isolated from liver and hepatoma had identical molecular weights and the same affinity for Sepharose-polyadenylate used in the isolation.
Mol Biol Rep 1977 Sep
PMID:Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells. 19 32

We have previously shown that cultured bovine pituitary or hypothalamic cells incorporate 3H-labeled amino acids into high molecular weight glycoproteins containing the antigenic determinants of both corticotropin (ACTH) and beta-endorphin. We now report resolution of this 3H-labeled ACTH/beta-endorphin-like material into two predominant size classes upon SDS polyacrylamide-gel electrophoresis with apparent molecular weights (Mr) of 41 500 +/- 1600 and 36 000 +/- 1100. Isoelectric focusing revealed these components to be basic proteins with apparent isoelectric points greater than 8.5. Overnight trypsinization generated a 3H-labeled fragment comigrating with synthetic beta-lipotropin (61-69) [beta-endorphin (1-9)] upon paper electrophoresis which was immunoprecipitable with antibody directed against the corresponding synthetic fragment. Limited trypsinization of bovine immunoreactive ACTH/beta-endorphin extracted from freshly obtained bovine hypothalamic and anterior pituitary tissue, generated fragments which possessed ACTH bioreactivity. Both bovine pituitary and hypothalamic derived material are similar with respect to these foregoing physiochemical parameters and appear to be larger than the reported forms in mouse pituitary.
Mol Cell Endocrinol 1979 Dec
PMID:Preliminary characterization of in vitro synthesized hypothalamic precursor ACTH/beta-endorphin-like material. 23 Jan 5

Yeast cells (Saccharomyces cerevisiae) were grown in the presence of [14C]phenylalanine and pulse-labelled with [3H]phenylalanine in the presence of cycloheximide. The proteins extractable into chroloform: methanol (2:1) were isolated from mitochondria and analysed by SDS gel filtration. Four protein fractions varying in molecular weight were separated. In order to identify the transcriptional origin and the site of protein synthesis ethidium bromide was used. Different sensitivity of protein syntheses to various concentrations of ethidium was shown. These data are discussed in relation to the possible presence of two classes of membrane-bound polyribosomes in mitochondria.
Mol Cell Biochem 1977 Feb 04
PMID:Intramitochondrial synthesis of membrane proteins in yeast: differential inhibition by ethidium. 32 93

A lambda phage has been isolated which specifically transduces the Escherichia coli pheS and pheT genes coding for the alpha and beta subunits of the phenylalanyl-tRNA synthetase (PRS). This phage transduces with high frequency (i) several temperature-sensitive PRS mutants to thermoresistance and (ii) a p-fluorophenylalanine resistant PRS mutant to sensitivity against this amino-acid analog. The in vitro PRS activities of such lysogens suggest that the alpha and beta subunits coded by the transducing phage complement the mutant host PRS-subunits in vivo by means of formation of hybrid enzymes. The transducing lambda phages were also used to infect UV light irradiated cells. The SDS-gel electrophoretic analysis of the proteins synthesized in such cells revealed that the phage codes at least for four different E. coli proteins. Two proteins with molecular weights of 94,000 and 38,000 daltons cross-reacted with an anti PRS serum and were thus identified as the beta and alpha subunits of PRS, respectively. A third protein with a molecular weight of 22,000 daltons is identical with the ribosomal initiation factor IF3 (Springer et al., 1977b). The other protein (Mr 78,000) is still unidentified.
Mol Gen Genet 1977 Apr 29
PMID:A specialized transducing lambda phage carrying the Escherichia coli genes for phenylalanyl-tRNA synthetase. 32 76

Analysis of lambda phage infection of the host mutant ER437 by SDS polyacrylamide gel electrophoresis and autoradiography has revealed altered expression of repressor and integration function (Int). We show that in this host Int as well as repressor synthesis is not dependent upon the lambdacIII gene product in the usual manner, nor is their synthesis turned off in the normal way.
Mol Gen Genet 1977 Oct 24
PMID:Repressor and int synthesis of bacteriophage lambda in the E. coli host mutant ER437. 34 Aug 86

The cytoplasmic 80s ribosomal proteins from the cells of yeast Sachharomyces cerevisiae were analysed by SDS two-dimensional polyacrylamide gel electrophoresis. Seventyfour proteins were identified and consecutively numbered from 1 to 74. Upon oxidation of the 80s proteins with performic acid, ten proteins (no. 15, 20, 35, 40, 44, 46, 49, 51, 54 and 55) were dislocated on the gel without change of the total number of protein spots. Five proteins (no. 8, 14, 16, 36 and 74) were phosphorylated in vivo as seen in 32P-labelling experiments. The large and small subunits separated in low magnesium medium were analyzed by the above gel electrophoresis. At least forty-five and twenty-eight proteins were assumed to be in the large and small subunits, respectively. All proteins found in the 80s ribosomes, except for no. 3, were detected in either subunit without appearance of new spots. The acidic protein no. 3 seems to be lost during subunit dissociation.
Mol Gen Genet 1978 Jul 04
PMID:Yeast ribosomal proteins. I. Characterization of cytoplasmic ribosomal proteins by two-dimensional gel electrophoresis. 35 32

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


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