Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The control of beta-galactosidase specified by the lactose transposon Tn951 (inserted into RP1 to give pGC9114) has been studied in Escherichia coli K12, Proteus mirabilis, Pseudomonas aeruginosa and Pseudomonas putida; in the first two species comparison could be made with Flac. In E. coli K12, the Tn951 and chromosomally encoded enzymes showed marked qualitative differences in regulatio, the former giving a substantially lower maximum induced level and induction ratio. Several parameters were slightly affected by strain background. In P. mirabilis, beta-galactosidase control determined by both Flac (in accord with earlier work) and pGC9114 was markedly different from E. coli in that maximal induced levels were about an order of magnitude lower and the induction ratio was reduced to 3 to 5. In Ps. aeruginosa and Ps. putida, Tn951-specified lac expression was qualitatively similar to that in P. mirabilis. Possible reasons for anomalous expression in Proteus and Pseudomonas are discussed.
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PMID:Expression of the lactose transposon Tn951 in Escherichia coli, Proteus and Pseudomonas. 625 Nov 61

The transposon Tn951 (lac) was introduced into the photosynthetic bacterium Rhodopseudomonas sphaeroides 2.4.1, which is normally Lac-, via the P-group plasmid RP1. beta-Galactosidase was produced constitutively in both chemotrophically and phototrophically grown cells, and the levels were found to be the same but low. Mutants were isolated, however, that were able to grow on lactose minimal medium and which expressed different levels of beta-galactosidase when grown chemotrophically or phototrophically. The beta-galactosidase levels found in all R. sphaeroides strains were much less than those found in Escherichia coli.
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PMID:Expression of the transposable lac operon Tn951 in Rhodopseudomonas sphaeroides. 629 Apr 58

None of the Agrobacterium tumefaciens and A. rubi strains tested produces detectable amounts of beta-galactosidase although they are capable of utilizing lactose as sole source of carbon. This opportunity was taken to investigate the expression of lac transposon Tn951 (Cornelis et al. 1978) in Agrobacterium with the ultimate goal of using this system to investigate alien gene expression. When the transposon was introduced with the help of a broad-host range plasmid, RP1, the transconjugants produced significant quantities of beta-galactosidase which was inducible by isopropyl-beta-D-thiogalactopyranoside. Tn951 was capable of restoring the Lac+ phenotype to an A. tumefaciens mutant not capable of using lactose. Cellobiose, a known inducer of aldohexopyranoside: cytochrome c oxidoreductase (which regulates the characteristic 3-ketolactose production in Agrobacterium; van Beeumen and De Ley (1968), had no effect on beta-galactosidase activity.
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PMID:Studies on Tn951 (lac+) expression in Agrobacterium. 632 25

The Tn10 tetR gene encodes the repressor that regulates transcription of the Tn10 tetracycline resistance determinant. We have determined the DNA sequence of the tetR gene and a 905 base pair region immediately 3' to tetR. The tetR gene is located on a 701 base pair HincII restriction fragment. Deletions at either end of this region eliminate synthesis of the wild-type TetR protein in E. coli minicells, and eliminate TetR activity as measured by repression of beta-galactosidase synthesis in tetA-lacZ operon fusion strains. Taken together, the DNA sequence and the genetic data indicate that tetR encodes a 207 amino acid protein with a calculated molecular weight of 23,328. This value is in good agreement with estimates of 23,000-25,000 based on electrophoretic mobility in SDS-polyacrylamide gels. There is 47% amino acid sequence homology between the deduced sequences of the Tn10 and RP1/Tn1721 TetR proteins. There is, in addition, significant amino acid sequence homology between an NH2-terminal region of the Tn10 TetR repressor and the DNA recognition regions of other DNA-binding proteins.
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PMID:Nucleotide sequence of the repressor gene of the TN10 tetracycline resistance determinant. 633 Jun 87

The lac operon shows anomalous expression in Proteus mirabilis: the maximal induced level is 10% or less of that in E. coli, while repression reduces this by a factor of only 2-5. We have sought to determine whether this effect relates in any way to CRP-mediated activation of expression, by comparing expression in P. mirabilis of lac operons (introduced for technical reasons on IncP1 plasmids) either regulatorily wild-type or bearing L8 or L8UV5. Derivatives of RP1 bearing L8UV5 were obtained by homogenotisation of pGC9114 (RP1::Tn951) in a L8UV5 background; while derivatives of RP4 bearing lac+, L8 or L8UV5 were obtained by Mu-mediated translocation of chromosomal regions bearing these alleles, following partial heat-induction of Mucts62 on pGM14 (RP4::Mucts62) in the appropriate hosts. These plasmids could be readily transferred to, and stably maintained in, the P. mirabilis strains employed. It was found that L8 reduced the maximal level of beta-galactosidase activity, and L8UV5 restored this activity to around wild-type, in P. mirabilis quantitatively very much as in E. coli. Nevertheless, the low maximal level of expression and high basal level characteristic of the former host were unchanged. The simplest explanation of these results is that P. mirabilis contains a protein that mimics the E. coli CRP protein in interacting with the appropriate DNA binding site and thereby stimulating transcription; and that the anomalous regulation of lac in this host is unconnected with the CRP system.
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PMID:Anomalous expression of the E. coli lac operon in Proteus mirabilis. I. Effects of L8 and L8 UV5. 644 Nov 2

Xanthomonas campestris, the producer of xanthan gum, possesses a beta-galactosidase of very low specific activity. Plasmid pGC9114 (RP1::Tn951), generated by the transposition of the lactose transposon Tn951 to RP1, was conjugally transferred into XN1, a nalidixic acid-resistant derivative of X. campestris NRRL B-1459S-4L. Transfer occurred on membrane filters and in broth. The beta-galactosidase gene of Tn951 was expressed in X. campestris. The specific activity of beta-galactosidase in transconjugants was over 200-fold higher than that in XN1, and transconjugants grew as well in lactose-based media as in glucose-based media. The lactose-utilizing transconjugants could potentially be used to produce xanthan gum from cheese whey.
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PMID:Genetic Construction of Lactose-Utilizing Xanthomonas campestris. 1634 64