Disease relevance of lambdap51

• Recognition sequences of repressor and polymerase in the operators of bacteriophage lambda [1].
• Previous experiments have shown that this operator contains multiple sites recognized by the lambda phage repressor [2].
• The kinetics of lambda l-strand repressor establishment RNA synthesis were measured from the y-cII region of induced tof- prophage [3].
• IS5 increases recombination in adjacent regions as shown for the repressor gene of coliphage lambda [4].
• If IHF binds to its DNA-binding site that has been placed into the P(ant) region of bacteriophage P22, it acts as a repressor of the ant (antirepressor) gene, leading to the formation of lysogens of Salmonella typhimurium [5].

High impact information on lambdap51

• The C-terminal domain of the repressor mediates dimerization as well as a dimer-dimer interaction that results in the cooperative binding of two repressor dimers to adjacent operator sites [6].
• A human dwarfism mutation that affects positive control in the related POU domain protein Pit-1 maps to the same region of the HTH motif as do positive control mutations in lambda repressor [7].
• Our mutagenesis studies also suggest limitations on amino acid substitutions that allow formation of the helix-turn-helix DNA binding motif found in repressor and in many other DNA binding regulatory proteins [8].
• A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor [8].
• We also find that the most important base pairs in the operator which enable repressor and Cro to discriminate between OR1 and OR3 are position 3 (for Cro) and positions 5 and 8 (for repressor) [9].

Chemical compound and disease context of lambdap51

• The sequences of insertions of the translocatable tetracycline-resistance element Tn10 into the repressor (cl) gene of bacteriophage lambda have been analyzed [10].
• A genetic system was developed in Escherichia coli to study leucine zippers with the amino-terminal domain of bacteriophage lambda repressor as a reporter for dimerization [11].
• We have used a tryptophan-requiring Escherichia coli auxotroph to replace the three tryptophan residues of lambda cI repressor with 5-hydroxy-L-tryptophan (5-OHTrp) [12].
• Spectral enhancement of proteins: biological incorporation and fluorescence characterization of 5-hydroxytryptophan in bacteriophage lambda cI repressor [12].
• Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor [13].

Biological context of lambdap51

• Each operator contains multiple repressor binding sites separated by A-T rich spacers [1].
• Autoregulation and function of a repressor in bacteriophage lambda [14].
• Completed DNA sequences and organization of repressor-binding sites in the operators of phage lambda [15].
• Control of bacteriophage lambda repressor establishment transcription: kinetics of l-strand transcription from the y-cII-oop-O-P region [3].
• Repressor establishment transcription and repressor mRNA synthesis from Prm (from induced cI- tof-, cIII- cI- tof- or cI- tof- cii- prophage) are amplified by gene dosage [3].

Anatomical context of lambdap51

• T lymphocyte response to bacteriophage lambda repressor cI protein. Recognition of the same peptide presented by Ia molecules of different haplotypes [16].
• The MHC class II molecule is the restricting element for the presentation of OVA and the lambda repressor from bacteriophage lambda to a panel of specific T cell hybridomas, as demonstrated by the blocking effect of anti-MHC class II mAb on the Ag-presenting function [17].
• We propose that this 13 bp deletion removes part of the binding site for a repressor protein which is abundant in adult erythroid cells [18].
• Unusual ribosome binding properties of mRNA encoding bacteriophage lambda repressor [19].
• Operator-binding studies made in vitro with purified mutant and wild-type repressors show that the binding curve of the former repressor is a rectangular hyperbola while that of the latter is sigmoid [20].

Associations of lambdap51 with chemical compounds

• Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions [11].
• By using a nonleaky promoter, we have achieved > 95% replacement of tryptophan in the repressor [12].
• Purified lambda repressor protein is shown to reduce the lambda DNA-directed synthesis of proteins in vitro as determined both by net amino-acid incorporation and by analysis of specific lambda-coded proteins resolved by sodium dodecyl sulfate/polyacrylamide slab gel electrophoresis [21].
• The assignment of arm resonances is made possible by the construction of mutant repressor genes containing successive NH2-terminal deletions [22].
• Additional contacts of lambda repressor and Cro protein with DNA, not observed by other chemical footprinting methods, are revealed by hydroxyl radical footprinting [23].

Physical interactions of lambdap51

• The cro protein binds to the same three sites in the right operator (OR) of bacteriophage lambda DNA as does the lambda repressor [24].

Regulatory relationships of lambdap51

• This approach allowed us to regulate the function of the lytic repressor at will and to prevent it from repressing cI, because lac repressor could not repress P(RM) in our constructs [25].
• This mutated operator structure accounts for the constitutive expression of their PR promoter either in cells overproducing the lambda repressor or in cells overproducing the cro gene product [26].

Other interactions of lambdap51

• The activity of the repressor is epistatic to the expression of gene tof coding for the antirepressor (Tof) [3].
• This sequence was determined by direct sequencing techniques and includes the codons for 11 carboxyterminal aminoacids of the cI product, the lambda repressor [27].
• Gene regulation at the right operator (OR) of bacteriophage lambda. II. OR1, OR2, and OR3: their roles in mediating the effects of repressor and cro [28].
• This work confirms that like repressor and Int, the 28.5-kilodalton protein, identified as Rex on HB gels, is postively regulated by the lambdacII and cIII products and negatively controlled Cro [29].
• The DNA fragments cloned into these plasmids are under control of the strong pL promoter, which can be regulated by the lambda repressor, and the antitermination activity of the N gene product [30].

Analytical, diagnostic and therapeutic context of lambdap51

• The fragment was identified as PL by restriction mapping, repressor binding, sequencing, and promoter location [31].
• The three different IgGs competed for binding to repressor in an enzyme-linked immunosorbent assay additivity test, which suggested that the three regions of conserved amino acids are probably located on the same side of the carboxyl domain of repressor and possibly close together in the tertiary structure [32].
• We describe a mutant lambda phage repressor that has specifically lost its activator function [33].
• Mutant frequencies obtained from drug treated and control animals were determined by in vitro packaging of the phage vector from genomic DNA followed by a colorimetric plaque assay to screen for phage in which the accompanying lacI repressor gene had mutated [34].
• Finally, the method is applied to the quantitative analysis of a hydroxyl radical footprint titration experiment to obtain the free energy of binding of the lambda repressor protein to the OR1 operator DNA sequence [35].

References