Recognition sequences of repressor and polymerase in the operators of bacteriophage lambda

Maniatis, Tom; Ptashne, Mark; Backman, Keith; Kleid, Dennis G.; Flashman, S.M.; Jeffrey, Andrea; Maurer, Russell

doi:10.1016/0092-8674(75)90018-5

Cited by 219 publications

(74 citation statements)

References 11 publications

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“…Since the base sequence of a substantial portion of the 5' untranslated and the complete 3' untranslated region of rat liver OTCase mRNA is known [28,32,331 it should be possible to compare homology between these regions of liver and intestinal OTCase mRNA once a cDNA clone for intestinal OTCase has been obtained. Analysis of the differences in regulatory elements in the gene is likely to be a much more difficult task since the gene appears to be at least (25)(26)(27)(28)(29)(30) x lo3 bases in length [38].…”

Section: Size Of 0 Tcase M R N Amentioning

confidence: 99%

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Comparison of ornithine transcarbamylase from rat liver and intestine

Wraight

Lingelbach

Hoogenraad

1985

European Journal of Biochemistry

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Ornithine transcarbamylase (OTCase) was purified from the small intestine of rat and the properties of the gut enzyme were compared with those of the enzyme from liver. The enzymes from both sources bound to the transition-state analog inhibitor, 6-N-(phosphonoacetyl)-L-ornithine, immobilized on Sepharose and eluted with carbamyl phosphate as a homogeneous preparation. The specific activities of the pure enzymes were 966 pmol min-' mg-' and 928 pmol min-l mg-' from liver and gut respectively, and the molecular mass, based on electrophoretic mobility, was 38000 Da. The isoelectric point of the enzymes from both sources was 7.3. The enzymes from both sources cross-react to the same extent with antibodies against the liver enzyme on Western transfers and the size of the mRNA was identical on Northern transfers probed with a cDNA for the livcr enzyme. Although OTCase is apparently the same gene product in both liver and gut, the enzyme levels respond differently to alterations in the protein content of the diet. OTCase in liver increased from 0.76 pin01 min-' pg-DNA on 15% casein to 1.3 pmol rnin-' pg-' DNA on 60% casein (P < 0.01) whereas in small intestine the level decreased from 8.8 nmol min-' pg DNA on 15% casein to 5.7 nmol min-' pg-' DNA on 60% casein ( P < 0.05). When expressed on a fresh-weight basis, the enzyme activity in liver shows the characteristic increase with increasing protein, whereas the activity in gut does not. The connection between these differences in gene expression and the different physiological roles of OTCase in liver and gut is discussed.Ornithine transcarbamylase (OTCase) catalyses the synthesis of citrulline from ornithine and carbamoyl phosphate. The enzyme is found in only two tissues, liver and intestine [I, 21, where it is localized in the matrix of mitochondria. However, the level of the enzyme in intestine is much less than in liver. The role of OTCase in the liver and intestine is apparently quite different. In liver, OTCase is involved in ammonia detoxification [3, 41 whereas in intestine it appears to be part of the arginine economy of an animal. The intestinal epithelium does not have a complete urea cycle and converts a significant proportion of glutamine nitrogen, derived from glutamine oxidation, to citrulline [5] via carbamoyl-phosphate synthetase and OTCase. The citrulline, synthesized by intestinal epithelium, is subsequently converted to arginine by peripheral tissues such as kidney [6 -81. We recently showed that intestinal citrulline synthesis is important in supplying arginine to intact animals, as selective inhibition of intestinal OTCase with a peptide derivative of the transition-state analog inhibitor, 6-N-(phosphonoacety1)-L-ornithine, significantly lowered blood arginine concentrations and severely inhibited the growth of young rats [9].Although the physical properties of the intestinal OTCase have apparently not been previously described and compared with OTCase from liver, both enzymes are probably encoded by a single X-linked gene. Thus, hyperammonemia, ...

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Section: Size Of 0 Tcase M R N Amentioning

confidence: 99%

“…A single cDNA clone, representing the entire length of precursor OTCase mRNA, was constructed from shorter cDNA clones. This 1500-base-pair fragment was isolated, purified [28] and nick-translated to a specific activity of 4 x 10' dpm/Fg [29].…”

Section: Analysis Of Rna By Northern Blottingmentioning

confidence: 99%

Comparison of ornithine transcarbamylase from rat liver and intestine

Wraight

Lingelbach

Hoogenraad

1985

European Journal of Biochemistry

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“…yeast tRNA and 0.1 % SDS. Hybridization to 2.5 x lo6 cpm of nick-translated probe [22] (2 x 10' cpm/pg DNA) was performed in 10 ml of prehybridization buffer minus glycine for 38 h. The blot was washed and autoradiograms were made as described [23].…”

Section: Blotting and Hybridization Proceduresmentioning

confidence: 99%

Cross‐linked proteins associated with a specific mRNA in the cytoplasm of HeLa cells

Ruždijić

Bag

Sells

1984

European Journal of Biochemistry

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Cytoplasmic messenger RNAs of eukaryotic cells are distributed between polysomal and post-polysomal fractions (free) as protein-bound complexes. These studies were designed to determine whether a specific mRNA isolated from different subcellular compartments is complexed with the same family of polypeptides. As a first approach we have examined the proteins associated with mRNA which codes for histone H4. To perform these experiments HeLa cells were exposed to ultraviolet light to cross-link in vivo polypeptides which are closely associated with nucleic acid. To identify the polypeptides associated with mRNA specific for histones a genomic probe for histone H4 mRNA was immobilized on epoxy-cellulose. By hybrid selection specific mRNPs containing histone mRNA were isolated. Our results reveal the existence of a number of polypeptides associated with both polysomal and post-polysomal histone mRNAs. In polysomal histone mRNA two polypeptides of M , = 49000 and 52500 were the major components. In contrast polypeptides of M,=43000 and 57000 were the major polypeptide components of post-polysomal (or free) histone mRNA. Furthermore, these results also suggest that the polypeptides associated with either polysomal or free H4 histone mRNA represent a subset of proteins found in poly(A)-free fractions or poly(A)-rich mRNA fractions.

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“…200 ng of this material was nick translated with [E~'P]~ATP to a specific activity of 4 x 10sdpm/pg [18].…”

Section: Nick Translationmentioning

confidence: 99%

Selection of a cDNA clone which contains the complete coding sequence for the mature form of ornithine transcarbamylase from rat liver: expression of the cloned protein in Escherichia coli Molecular cloning of rat ornithine transcarbamylase. Molecular cloning of rat ornithine transcarbamylase

et al. 1984

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A cDNA clone corresponding to the mature form of ornithine transcarbamylase (OTCase) was selected from a rat liver cDNA library constructed in bacteriophage 2gt10. OTCase clones were selected using a synthetic DNA probe of 15 bases corresponding to the 3' end of the OTCase mRNA [ Horwich, A. L., Kraus, J. P., Williams, K., Kalousek, F., Konigsberg, W.& Rosenberg, L. E. (1983) Proc. Nut1 Acad. Sci. USA, 80, 4258-42621. Putative OTCase clones were subcloned into the expression vector, pUC9, and the identity of inserts confirmed by colony immunoassay and by electrophoretic transfer of cloned proteins from sodium dodecyl sulphate/polyacrylamide gels to nitrocellulose filters followed by probing with monospecific anti-OTCase antibodies and 12sI-labelled protein A. A clone corresponding to the full-length mature form of rat liver OTCase (plus 15 amino acids from Eschevichia coli P-galactosidasc) was obtained and the identity of

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Recognition sequences of repressor and polymerase in the operators of bacteriophage lambda

Cited by 219 publications

References 11 publications

Comparison of ornithine transcarbamylase from rat liver and intestine

Comparison of ornithine transcarbamylase from rat liver and intestine

Cross‐linked proteins associated with a specific mRNA in the cytoplasm of HeLa cells

Selection of a cDNA clone which contains the complete coding sequence for the mature form of ornithine transcarbamylase from rat liver: expression of the cloned protein in Escherichia coli Molecular cloning of rat ornithine transcarbamylase. Molecular cloning of rat ornithine transcarbamylase

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