Literature DB >> 6790520

Position of the lacZX90 mutation and hybridization between complete and incomplete beta-galactosidase.

W Mandecki, A V Fowler, I Zabin.   

Abstract

The position of the termination codon in lacZX90 was determined by isolation of a lac+ revertant. Lysine was found to replace tyrosine at position 1,012 of beta-galactosidase, indicating that X90 protein lacked the carboxyl-terminal 10 residues. A heat- and urea-sensitive hybrid enzyme was formed in vivo when supC, which supplies tyrosine to the position in the polypeptide corresponding to the nonsense codon, was used to suppress lacZX90. This result shows that suppression that adds back the original amino acid may not lead to the production of the wild-type enzyme if the latter is multimeric, because incomplete chains can be incorporated into the oligomer.

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Year:  1981        PMID: 6790520      PMCID: PMC216095          DOI: 10.1128/jb.147.2.694-697.1981

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  20 in total

1.  In vivo complementation between wild-type and mutant -galactosidase in Escherichia coli.

Authors:  B G Hall
Journal:  J Bacteriol       Date:  1973-04       Impact factor: 3.490

2.  Beta-galactosidase. Rates of synthesis and degradation of incomplete chains.

Authors:  S Lin; I Zabin
Journal:  J Biol Chem       Date:  1972-04-10       Impact factor: 5.157

3.  -Galactosidase: immunological activity of ribosome-bound, growing polypeptide chains.

Authors:  J Hamlin; I Zabin
Journal:  Proc Natl Acad Sci U S A       Date:  1972-02       Impact factor: 11.205

4.  [Identification, by in vitro complementation and purification, of a peptide fraction of Escherichia coli beta-galactosidase].

Authors:  A Ullmann; D Perrin; F Jacob; J Monod
Journal:  J Mol Biol       Date:  1965-07       Impact factor: 5.469

5.  In vivo degradation of nonsense fragments in E. coli.

Authors:  R Goldschmidt
Journal:  Nature       Date:  1970-12-19       Impact factor: 49.962

6.  Beta-galactosidase: orientation and the carboxyl-terminal coding site in the gene.

Authors:  J L Brown; D M Brown; I Zabin
Journal:  Proc Natl Acad Sci U S A       Date:  1967-09       Impact factor: 11.205

7.  The effect of urea on subunit interactions of beta-galactosidase from Escherichia coli K12.

Authors:  S Shifrin; E Steers
Journal:  Biochim Biophys Acta       Date:  1967-04-11

8.  Co-linearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains.

Authors:  A V Fowler; I Zabin
Journal:  Science       Date:  1966-11-25       Impact factor: 47.728

9.  beta-galactosidase omega-complementation with a small cyanogen bromide peptide.

Authors:  J K Welply; W Mandecki; A V Fowler; I Zabin
Journal:  Biochem Biophys Res Commun       Date:  1980-03-13       Impact factor: 3.575

10.  Hybrid enzyme molecules reconstituted from mixtures of wild-type and mutant Escherichia coli -galactosidase.

Authors:  F Melchers; W Messer
Journal:  J Mol Biol       Date:  1971-10-28       Impact factor: 5.469

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  4 in total

1.  Identification of a nuclear localization signal of a yeast ribosomal protein.

Authors:  R B Moreland; H G Nam; L M Hereford; H M Fried
Journal:  Proc Natl Acad Sci U S A       Date:  1985-10       Impact factor: 11.205

2.  Genetic studies on the beta subunit of Escherichia coli RNA polymerase. II. Evidence that large N-terminal amber fragments of the beta subunit interfere with RNA polymerase function.

Authors:  V Nene; R E Glass
Journal:  Mol Gen Genet       Date:  1982

3.  Characteristics of the beta-galactosidase-carboxypeptidase complex in GM1-gangliosidosis and beta-galactosialidosis fibroblasts.

Authors:  R M D'Agrosa; M Hubbes; S Zhang; R Shankaran; J W Callahan
Journal:  Biochem J       Date:  1992-08-01       Impact factor: 3.857

4.  E.coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism.

Authors:  M Robert-Le Meur; C Portier
Journal:  EMBO J       Date:  1992-07       Impact factor: 11.598

  4 in total

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