Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Female lactose adapted rats were kept for 10 days on human milk (HM), a milk diet adapted to human milk (MD1), and a milk diet rich in protein and phosphate (MD2), the lactose supply being always the same. In the caecum, colon and faeces, the pH value, the phosphorus content, the buffer capacity and the numbers of microorganisms with proteolytic activity (Bacteroides, Klebsiella, Proteus) were lower and the lactose concentration and the beta-galactosidase activity were higher on HM and MD1 than on MD2.
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PMID:[The degradation of lactose in the intestines of rats on human and cow's milk diets]. 647 40

The small DNA binding protein Fis is involved in several different biological processes in Escherichia coli. It has been shown to stimulate DNA inversion reactions mediated by the Hin family of recombinases, stimulate integration and excision of phage lambda genome, regulate the transcription of several different genes including those of stable RNA operons, and regulate the initiation of DNA replication at oriC. fis has also been isolated from Salmonella typhimurium, and the genomic sequence of Haemophilus influenzae reveals its presence in this bacteria. This work extends the characterization of fis to other organisms. Very similar fis operon structures were identified in the enteric bacteria Klebsiella pneumoniae, Serratia marcescens, Erwinia carotovora, and Proteus vulgaris but not in several nonenteric bacteria. We found that the deduced amino acid sequences for Fis are 100% identical in K. pneumoniae, S. marcescens, E. coli, and S. typhimurium and 96 to 98% identical when E. carotovora and P. vulgaris Fis are considered. The deduced amino acid sequence for H. influenzae Fis is about 80% identical and 90% similar to Fis in enteric bacteria. However, in spite of these similarities, the E. carotovora, P. vulgaris, and H. influenzae Fis proteins are not functionally identical. An open reading frame (ORF1) preceding fis in E. coli is also found in all these bacteria, and their deduced amino acid sequences are also very similar. The sequence preceding ORF1 in the enteric bacteria showed a very strong similarity to the E. coli fis P region from -53 to +27 and the region around -116 containing an ihf binding site. Both beta-galactosidase assays and primer extension assays showed that these regions function as promoters in vivo and are subject to growth phase-dependent regulation. However, their promoter strengths vary, as do their responses to Fis autoregulation and integration host factor stimulation.
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PMID:Identification and characterization of the fis operon in enteric bacteria. 981 52

The IgA-degrading metalloprotease, ZapA, of the urinary tract pathogen Proteus mirabilis is co-ordinately expressed along with other proteins and virulence factors during swarmer cell differentiation. In this communication, we have used zapA to monitor IgA protease expression during the differentiation of vegetative swimmer cells to fully differentiated swarmer cells. Northern blot analysis of wild-type cells and beta-galactosidase measurements using a zapA:lacZ fusion strain indicate that zapA is fully expressed only in differentiated swarmer cells. Moreover, the expression of zapA on nutrient agar medium is co-ordinately regulated in concert with the cycles of cellular differentiation, swarm migration and consolidation that produce the bull's-eye colonies typically associated with P. mirabilis. ZapA activity is not required for swarmer cell differentiation or swarming behaviour, as ZapA- strains produce wild-type colony patterns. ZapA- strains fail to degrade IgA and show decreased survival compared with the wild-type cells during infection in a mouse model of ascending urinary tract infection (UTI). These data underscore the importance of the P. mirabilis IgA-degrading metalloprotease in UTI. Analysis of the nucleotide sequences adjacent to zapA reveals four additional genes, zapE, zapB, zapC and zapD, which appear to possess functions required for ZapA activity and IgA proteolysis. Based on homology to other known proteins, these genes encode a second metalloprotease, ZapE, as well as a ZapA-specific ABC transporter system (ZapB, ZapC and ZapD). A model describing the function and interaction of each of these five proteins in the degradation of host IgA during UTI is presented.
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PMID:ZapA, the IgA-degrading metalloprotease of Proteus mirabilis, is a virulence factor expressed specifically in swarmer cells. 1036 Dec 85

Expression of Proteus mirabilis urease is governed by UreR, an AraC-like positive transcriptional activator. A poly(A) tract nucleotide sequence, consisting of A(6)TA(2)CA(2)TGGTA(5)GA(6)TGA(5), is located 16 bp upstream of the sigma(70)-like ureR promoter P2. Since poly(A) tracts of DNA serve as binding sites for the gene repressor histone-like nucleoid structuring protein (H-NS), we measured beta-galactosidase activity of wild-type Escherichia coli MC4100 (H-NS(+)) and its isogenic derivative ATM121 (hns::Tn10) (H-NS(-)) harboring a ureR-lacZ operon fusion plasmid (pLC9801). beta-Galactosidase activity in the H-NS(-) host strain was constitutive and sevenfold greater (P < 0.0001) than that in the H-NS(+) host. A recombinant plasmid containing cloned P. mirabilis hns was able to complement and restore repression of the ureR promoter in the H-NS(-) host when provided in trans. Deletion of the poly(A) tract nucleotide sequence from pLC9801 resulted in an increase in beta-galactosidase activity in the H-NS(+) host to nearly the same levels as that observed for wild-type pLC9801 harbored by the H-NS(-) host. Urease activity in strains harboring the recombinant plasmid pMID1010 (encoding the entire urease gene cluster of P. mirabilis) was equivalent in both the H-NS(-) background and the H-NS(+) background in the presence of urea but was eightfold greater (P = 0.0001) in the H-NS(-) background in the absence of urea. We conclude that H-NS represses ureR expression in the absence of urea induction.
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PMID:H-NS is a repressor of the Proteus mirabilis urease transcriptional activator gene ureR. 1076 73

The genus Proteus belongs to the tribe of Proteae in the family of Enterobacteriaceae, and consists of five species: P. mirabilis, P. vulgaris, P. morganii, P. penneri and P. myxofaciens. They are distinguished from the rest of Enterobacteriaceae by their ability to deaminate phenylalanine and tryptophane. They hydrolyze urea and gelatin and fail to ferment lactose, mannose, dulcitol and malonate; and do not form lysine and arginine decarboxylase or beta-galactosidase [1]. Colonies produce distinct "burned chocolate" odor and frequently show the characteristics of swarming motility on solid media. P. mirabilis, P. vulgaris and P. morganii are widely recognized human pathogens. They have been isolated from urinary tract infections, wounds, ear, and nosocomial bacteremic infections, often in immuncompromised patients [2-6]. P. myxofaciens has no clinical interest to this time. P. penneri as species nova was nominated by the recommendation of Hickman and co-workers [7]. Formerly it was recognized as P. vulgaris biogroup 1 or indole negative P. vulgaris [8, 9]. Although it has been less commonly isolated from clinical samples than the other three human pathogenic Proteus species, it has nevertheless been connected with infections of the urinary tract, wounds and has been isolated from the feces of both healthy and diarrheic individuals [10-12]. Potential virulence factors responsible for virulence of Proteae are: IgA protease, urease, type3 fimbriae associated with MR/K haemagglutinins of at least two antigenic types, endotoxin, swarming motility and HlyA and/or HpmA type hemolysins [for review see ref. 13]. In the followings we give a survey of accumulated concepts about the position and characteristics of HlyA type alpha-hemolysins both in general and with emphasis on virulence functions in the tribe of Proteae.
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PMID:Proteus virulence: involvement of the pore forming alpha-hemolysin (a short review). 1105 65

Falkow, Stanley (Walter Reed Army Institute of Research, Washington, D.C.), J. A. Wohlhieter, R. V. Citarella, and L. S. Baron. Transfer of episomic elements to Proteus. I. Transfer of F-linked chromosomal determinants. J. Bacteriol. 87:209-219. 1964.-F-linked lac(+) genes may be transferred from Escherichia coli to several species of Proteus by conjugation. Usually the transferred genetic elements are markedly unstable in Proteus, but repeated plating permits the selection of relatively stable Proteus lac(+) strains. Proteus strains carrying F-linked lac(+) markers are heterogenotes and limited donors for lac(+). In addition, both the fertility and lac(+) property may be eliminated from Proteus by treatment with acridine orange. Escherichia and Proteus possess very different overall deoxyribonucleic acid (DNA) base compositions. In CsCl density gradients of DNA extracted from Proteus lac(+) strains, the acquisition of Escherichia genes by Proteus may be correlated with the addition of a physically recognizable high molecular weight, native DNA fraction of Escherichia base composition. Proteus lac(+) strains synthesize a beta-galactosidase which is indistinguishable from E. coli enzyme by several criteria. Despite this specificity, the regulatory functions of Escherichia lac(+) genes appear to be impaired in Proteus.
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PMID:TRANSFER OF EPISOMIC ELEMENTS TO PROTEUS. I. TRANSFER OF F-LINKED CHROMOSOMAL DETERMINANTS. 1410 56

One hundred and fourteen strains of non-lactose fermenters and 127 lactose fermenters on MacConkey's agar have been compared in the 5% and 1% lactose tests and in beta-galactosidase production, using ortho-nitro-phenyl-beta-D-galactopyranoside (O.N.P.G.) as a test substance. The superiority of the O.N.P.G. test in the number of positive results and its rapidity is shown. In general, late or non-lactose fermenting strains of genera, usually lactose-positive, yield a rapidly positive O.N.P.G. reaction. Forty-one wild strains of Salmonella, Proteus, Providencia, and Pseudomonas aeruginosa were found negative in all three tests. Of 1,075 stock strains of Salmonella examined in the O.N.P.G. test, all were negative except nine; four of these were lactose-positive strains. For practical purposes, Salmonella strains in Great Britain may be regarded as O.N.P.G. negative. Among 100 stock strains of Arizona there was considerable variation of behaviour in the O.N.P.G. test and in the 5% and 1% lactose tests. Most strains of Arizona can be considered to yield a positive O.N.P.G. test but a minority give a negative result. The test is recommended for routine use in the differentiation of Salmonella from other enterobacteria and for use in bacterial identification. The 5% lactose fermentation test in parallel is suggested when the O.N.P.G. test is used for isolating routine pathogens, because organisms such as Shigella sonnei, Shigella dysenteriae 1, and Pasteurella pseudotuberculosis are O.N.P.G. positive.
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PMID:BETA-GALACTOSIDASE AND LACTOSE FERMENTATION IN THE IDENTIFICATION OF ENTEROBACTERIA INCLUDING SALMONELLAE. 1414 33

The intracellular concentration of the Escherichia coli factor for inversion stimulation (Fis), a global regulator of transcription and a facilitator of certain site-specific DNA recombination events, varies substantially in response to changes in the nutritional environment and growth phase. Under conditions of nutritional upshift, fis is transiently expressed at very high levels, whereas under induced starvation conditions, fis is repressed by stringent control. We show that both of these regulatory processes operate on the chromosomal fis genes of the enterobacteria Klebsiella pneumoniae, Serratia marcescens, Erwinia carotovora, and Proteus vulgaris, strongly suggesting that the physiological role of Fis is closely tied to its transcriptional regulation in response to the nutritional environment. These transcriptional regulatory processes were previously shown to involve a single promoter (fis P) preceding the fis operon in E. coli. Recent work challenged this notion by presenting evidence from primer extension assays which appeared to indicate that there are multiple promoters upstream of fis P that contribute significantly to the expression and regulation of fis in E. coli. Thus, a rigorous analysis of the fis promoter region was conducted to assess the contribution of such additional promoters. However, our data from primer extension analysis, S1 nuclease mapping, beta-galactosidase assays, and in vitro transcription analysis all indicate that fis P is the sole E. coli fis promoter in vivo and in vitro. We further show how certain conditions used in the primer extension reactions can generate artifacts resulting from secondary annealing events that are the likely source of incorrect assignment of additional fis promoters.
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PMID:Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fis P) in Escherichia coli. 1467 32


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