Disease relevance of cII

• Nucleotide sequence of cro, cII and part of the O gene in phage lambda DNA [1].
• To obtain this protein, the cII gene was cloned into a plasmid vector carrying the strong, regulatable lambda phage promoter PL such that it was overproduced to levels approaching 5% of cellular protein [2].
• The gene for the Harvey murine sarcoma virus (Ha-MuSV) p21ras protein was fused to the amino-terminal portion of the bacteriophage lambda cII gene on the expression vector pJL6 [3].
• An Escherichia coli HtpR- strain has been identified that greatly stabilizes these highly unstable cII mutants [4].
• Lambda cII expression from an induced prophage is increased twofold in the presence of a large excess of anti-OOP RNA [5].

High impact information on cII

• Proper conformation of the transcripts is essential for activity, since put mutations that prevent the formation of predicted RNA stems prevented antitermination, and suppressor mutations that restore the stems restored antitermination [6].
• In vivo experiments with gene-fusion plasmids were used to examine the ability of specific areas of the rrnG control region to convert an ordinary transcription complex into antitermination transcription complex [7].
• We conclude that the E. coli ribosomal RNA operons possess an antitermination system similar to that used by the bacteriophage lambda [7].
• This may result from the deficiency of cII protein caused by its decreased stability, since cII product is required for establishment of lysogeny [8].
• We demonstrate that cII is a DNA binding protein that selectively interacts with a repeat sequence in the -35 region of the promoter [9].

Chemical compound and disease context of cII

• Hypothetical amino-acid sequences of proteins coded by the cro gene of phage 434 and the cII gene of phage lambda, as well as NH2-terminal amino-acid sequences of the cI protein of phage 434 and the O protein of phage lambda, have been deduced solely on the basis of the DNA sequence [10].
• When restriction fragments carrying the promoter-terminator segments from each of these phages were inserted into the trp operon, both responded identically to cII activation, and both caused termination [11].
• Last, in contrast to lambda cII, the C1 protein exhibited little cooperativity with Escherichia coli RNA polymerase for DNA binding, but because of its stronger inherent binding ability, achieved an overall promoter affinity similar to that observed for cII at its cognate promoter signals [12].
• RNA structural elements for expression in Escherichia coli. Alpha 1-antitrypsin synthesis using translation control elements based on the cII ribosome-binding site of phage lambda [13].

Biological context of cII

• Mutations that alter the DNA binding site for the bacteriophage lambda cII protein and affect the translation efficiency of the cII gene [14].
• Since the cII protein of ctr-3 has the same primary sequence as that of lambda cII3059, the cII- phenotype of lambda cII3059 can be explained entirely by the deficiency of translating cII mRNA [14].
• The ctr mutations lie in an overlapping regulatory region which contains, in addition to sequence elements that influence the rate of cII translation, a region to which cII protein binds to activate transcription from the PRE promoter [14].
• Plasmids were constructed to supply cII-coded protein for activation of the phage promoter pI [15].
• The fusion was such that transcription was controlled by the well-regulated phage lambda pL promoter, and translation initiated in the cII gene continued in frame into the ras gene sequences that code for p21 [3].

Anatomical context of cII

• In p39-AS, the rho leader is completely absent, and the lambda cII ribosome binding site replaces that of rho [16].
• Analysis of the cII mutational spectrum within the mammary tumor genomic DNA demonstrated a >6-fold elevation in transversion mutation frequency, resulting in a highly unusual inversion of the transition/transversion ratio characteristic of normal epithelium; frameshift mutation frequencies were unaltered [17].
• In the small intestine, PhIP increased the cII MF to four-fold that of the control, but IQ, MeIQ, and Trp-P-2 did not have a significant mutagenic effect [18].
• In the cecum, cII MFs induced by IQ and MeIQ were 1.9 and 2.7 times those in the control, respectively [18].
• To evaluate the in vivo mutagenicity of 3-NBA, we analyzed the mutant frequency (MF) in the cII gene of various organs (lung, liver, kidney, bladder, colon, spleen, and testis) in lambda/lacZ transgenic mice (Muta Mouse) after intraperitoneal treatment with 3-NBA (25 mg/kg body weight injected once a week for 4 weeks) [19].

Associations of cII with chemical compounds

• The cII mutational spectra in these tissues consisted mostly of G/C-->A/T transitions, a large fraction of which occurred at CpG dinucleotides [20].
• We demonstrate that cII in solution is a tetrameric protein and that it undergoes specific processing at its NH2-terminal end [21].
• Of 314 mutants, 182 (58%) had independent mutations, 74 (23.5%) appeared clonal, and 58 (18.5%) showed no cII mutations [22].
• Comparison of mutant frequencies at the transgenic lambda LacI and cII/cI loci in control and ENU-treated Big Blue mice [23].
• The helix-bend-helix motif rationalizes genetic analysis of N-dependent transcriptional antitermination and extends the structural repertoire of arginine-rich domains observed among mammalian immunodeficiency viruses [24].

Physical interactions of cII

• The bacteriophage lambda cIII gene product regulates the lysogenic pathway by stabilizing the lambda cII regulatory protein [25].

Other interactions of cII

• Our results suggest that positive regulation by cII/cIII involves initiation of new RNA chains through activation of promoter sites [26].
• The cII-independent expression of the phage lambda int gene in RNase III-defective E. coli [27].
• As expected of a cII mutation, lambdacIIts612 is unable to stimulate either cI repressor or Int synthesis during the establishment of lysogeny [28].

Analytical, diagnostic and therapeutic context of cII

• We have constructed a promoter down mutation, paq-1, by changing a single base pair in the putative cII binding site of the promoter by oligonucleotide site-directed mutagenesis [29].
• The tp4 mutation was mapped in the cY-cII region, and complementation tests indicated that tp4 affects the diffusible product of the cII gene [30].
• The expressed protein is a fusion between the N-terminal 13 amino acids of the cII gene, 8 amino acids resulting from the ligation procedure, and the 180 amino acids that comprise the HIV-2 Nef sequence from the NIH-Z strain [31].

References