scholarly journals The role of the regulator-gene product (repressor) in catabolite repression of β-galactosidase synthesis in Escherichia coli

1968 ◽  
Vol 106 (2) ◽  
pp. 339-343 ◽  
Author(s):  
J. Palmer ◽  
V. Moses
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Catabolite Repression ◽  
Lac Repressor ◽  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Amber Suppressor ◽  
Transient Repression ◽  
I Gene

1. The specific role of the lac repressor (i-gene product) in transient catabolite repression evoked by the introduction of glucose into the medium has been investigated in Escherichia coli by using mutants of the i-gene. 2. A temperature-sensitive mutant (iTL) is normally inducible and demonstrates transient repression when grown at 32°. At 42° it is about 20% constitutive and transient catabolite repression is abolished. 3. A strain carrying an amber suppressor-sensitive mutation in the i-gene is phenotypically constitutive and also fails to show transient catabolite repression. 4. Insertion of Flaci+ into this strain restores both inducibility and transient repression. 5. It is concluded that the i-gene product interacts with the catabolite co-repressor in such a way that its affinity for the operator is increased.

scholarly journals The Bacteriophage P1 hot Gene Product Can Substitute for the Escherichia coli DNA Polymerase III θ Subunit

2005 ◽  
Vol 187 (16) ◽  
pp. 5528-5536 ◽  
Author(s):  
Anna K. Chikova ◽  
Roel M. Schaaper
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Dna Polymerase ◽  
Temperature Sensitive ◽  
Bacteriophage P1 ◽  
Replication Errors ◽  
Pol Iii ◽  
Dna Replication Errors ◽  
Replication Factors

ABSTRACT The θ subunit (holE gene product) of Escherichia coli DNA polymerase (Pol) III holoenzyme is a tightly bound component of the polymerase core. Within the core (α-ε-θ), the α and ε subunits carry the DNA polymerase and 3′ proofreading functions, respectively, while the precise function of θ is unclear. holE homologs are present in genomes of other enterobacteriae, suggestive of a conserved function. Putative homologs have also been found in the genomes of bacteriophage P1 and of certain conjugative plasmids. The presence of these homologs is of interest, because these genomes are fully dependent on the host replication machinery and contribute few, if any, replication factors themselves. To study the role of these θ homologs, we have constructed an E. coli strain in which holE is replaced by the P1 homolog, hot. We show that hot is capable of substituting for holE when it is assayed for its antimutagenic action on the proofreading-impaired dnaQ49 mutator, which carries a temperature-sensitive ε subunit. The ability of hot to substitute for holE was also observed with other, although not all, dnaQ mutator alleles tested. The data suggest that the P1 hot gene product can substitute for the θ subunit and is likely incorporated in the Pol III complex. We also show that overexpression of either θ or Hot further suppresses the dnaQ49 mutator phenotype. This suggests that the complexing of dnaQ49-ε with θ is rate limiting for its ability to proofread DNA replication errors. The possible role of hot for bacteriophage P1 is discussed.

The role of lac operon and lac repressor in the induction using lactose for the expression of periplasmic human interferon-α2b by Escherichia coli

2011 ◽  
Vol 62 (4) ◽  
pp. 1427-1435 ◽  
Author(s):  
Joo Shun Tan ◽  
Ramakrishnan Nagasundara Ramanan ◽  
Tau Chuan Ling ◽  
Shuhaimi Mustafa ◽  
Arbakariya B. Ariff
Keyword(s):  
Escherichia Coli ◽  
Lac Repressor ◽  
Human Interferon ◽  
Lac Operon ◽  
Interferon Α2b

An amber mutation in the gene encoding the beta' subunit of Escherichia coli RNA polymerase

1982 ◽  
Vol 152 (2) ◽  
pp. 736-746
Author(s):  
S P Ridley ◽  
M P Oeschger
Keyword(s):  
Escherichia Coli ◽  
High Temperature ◽  
Rna Polymerase ◽  
Coli Strain ◽  
Beta Subunit ◽  
Temperature Sensitive ◽  
Amber Mutation ◽  
Gene Encoding ◽  
Amber Suppressor

An Escherichia coli strain carrying an amber mutation (UAG) in rpoC, the gene encoding the beta prime subunit of RNA polymerase, was isolated after mutagenesis with nitrosoguanidine. The mutation was moved into an unmutagenized strain carrying the supD43,74 allele, which encodes a temperature-sensitive su1 amber suppressor, and sue alleles, which enhance the efficiency of the suppressor. In this background, beta prime is not synthesized at high temperature. Suppression of the mutation by the non-temperature-sensitive amber suppressor su1+ yields a protein which is functional at all temperatures examined (30, 37, and 42 degrees C).

scholarly journals Role of Virulence Factors in Resistance of Avian Pathogenic Escherichia coli to Serum and in Pathogenicity

2003 ◽  
Vol 71 (1) ◽  
pp. 536-540 ◽  
Author(s):  
Melha Mellata ◽  
Maryvonne Dho-Moulin ◽  
Charles M. Dozois ◽  
Roy Curtiss ◽  
Peter K. Brown ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Virulence Factors ◽  
Bacterial Resistance ◽  
Serum Resistance ◽  
Temperature Sensitive ◽  
E Coli ◽  
Pathogenic Escherichia Coli ◽  
K1 Capsule

ABSTRACT In chickens, colibacillosis is caused by avian pathogenic Escherichia coli (APEC) via respiratory tract infection. Many virulence factors, including type 1 (F1A) and P (F11) fimbriae, curli, aerobactin, K1 capsule, and temperature-sensitive hemagglutinin (Tsh) and plasmid DNA regions have been associated with APEC. A strong correlation between serum resistance and virulence has been demonstrated, but roles of virulence factors in serum resistance have not been well elucidated. By using mutants of APEC strains TK3, MT78, and χ7122, which belong to serogroups O1, O2, and O78, respectively, we investigated the role of virulence factors in resistance to serum and pathogenicity in chickens. Our results showed that serum resistance is one of the pathogenicity mechanisms of APEC strains. Virulence factors that increased bacterial resistance to serum and colonization of internal organs of infected chickens were O78 lipopolysaccharide of E. coli χ7122 and the K1 capsule of E. coli MT78. In contrast, curli, type 1, and P fimbriae did not appear to contribute to serum resistance. We also showed that the iss gene, which was previously demonstrated to increase resistance to serum in certain E. coli strains, is located on plasmid pAPEC-1 of E. coli χ7122 but does not play a major role in resistance to serum for strain χ7122.

scholarly journals The role of ribonuclease II in the maturation of precursor 16S ribosomal ribonucleic acid in Escherichia coli

1974 ◽  
Vol 140 (3) ◽  
pp. 443-450 ◽  
Author(s):  
John R. Dean ◽  
John Sykes
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Maximum Activity ◽  
Exponential Phase ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Experimental Conditions ◽  
Inhibition Of Growth ◽  
Ribosomal Ribonucleic Acid

The suggested involvement of ribonuclease II in the maturation of rRNA has been examined directly by determining the activity of the enzyme and the amount of p16S rRNA in cell-free extracts from Escherichia coli A19 and its temperature-sensitive derivative N464 grown under experimental conditions designed to vary the amounts of enzyme and precursor independently. In strain A19 the enzyme showed maximum activity in circumstances where the amount of p16S rRNA was normal (e.g. exponential-phase cells) or raised eight times (e.g. during inhibition of growth by methionine starvation of the relaxed auxotroph or by chloramphenicol or puromycin treatment). In strain N464 at the non-permissive temperature the ribonuclease II activity may be decreased by 50% without effect upon the amount of p16S rRNA, whereas in methionine starvation of this strain the enzyme activity is at a maximum and the p16S rRNA is eight times that in exponential-phase cells. These observations are discussed in relation to the previously implied role of ribonuclease II in the maturation of rRNA within ribosome precursors.

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