Structure and expression of the human haptoglobin locus.

Bensi, G; Raugei, Giovanni; Klefenz, H.; Cortese, Riccardo

doi:10.1002/j.1460-2075.1985.tb02325.x

Cited by 147 publications

(94 citation statements)

References 22 publications

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“…A synthetic 36mer oligonucleotide complementary to the codons 18-30 (5 ' -TTGCTGCTGCTGGAAGAAGGCA-GTGCCCAGCTCCTG-3 ' ) was synthesized by Dr Igolen, Institut Pasteur de Paris. It was labeled in 5 ' by polynucleotide kinase [ 151, annealed to poly(A)-containing mRNA purified from a carbohydrate-fed rat liver, then extended by reverse transcriptase [16]. A 106 base major elongation product was purified by denaturing polyacrylamide gel electrophoresis and sequenced according to Maxam and Gilbert [lS].…”

Section: Methodsmentioning

confidence: 99%

Complete nucleotide and deduced amino acid sequences of rat L‐type pyruvate kinase

et al. 1986

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Four overlapping cDNA clones for L‐type pyruvate kinase (PK‐L) were isolated from carbohydrate‐induced rat liver cDNA libraries. They contained all the coding sequence of the enzyme from the 7th codon and the entire 3'‐untranslated extension up to the poly(A) tail. The sequence of the first 7 codons and that of the 5'‐untranslated region were determined by primer extension. The analyzed PK‐L mRNA has 19 5'‐untranslated bases, 1629 coding bases and 1281 3'‐untranslated bases without the poly(A) tail; it corresponds to the heavier, 3.2 kb species of the L‐type mRNAs. The codons for the phosphorylatable site are, located at the 5'‐end of the messenger. The unusually long 3'‐untranslated extension contains a repetitive element complementary to the ‘brain‐specific’ identifier sequence described by Sutcliffe et al. [(1982) Proc. Natl. Acad. Sci. USA 79, 4942‐4946].

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Section: Methodsmentioning

confidence: 99%

Complete nucleotide and deduced amino acid sequences of rat L‐type pyruvate kinase

et al. 1986

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“…Primer extensions were done according to Bensi et al (1985). Methods to map the 5' end of the PRP28 transcript were carried out on wild-type RNA.…”

Section: Phd3mentioning

confidence: 99%

A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family.

Strauss¹,

Guthrie²

1991

Genes Dev.

142

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We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which the first step of mRNA splicing is inhibited. The growth and splicing defects are recessive and cosegregate, thus defining a single essential gene (PRP28). The wild-type PRP28 gene was cloned, and sequence analysis reveals extensive homology to a family of proteins that are thought to function as ATP-dependent RNA helicases. The cold sensitivity is caused by a glycine-to-glutamic acid change in a conserved sequence motif. Interestingly, double mutants containing conditional alleles of PRP28 and PRP24, which encodes a U6 snRNA-binding protein, are inviable. In addition, a suppressor of prp28-1 is a mutant allele of PRP8, which encodes a U5 protein, thus linking PRP28 with U5. These data are consistent with a scenario in which PRP28 acts to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing.

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“…Its sequence was S'TTGCTGCTGCTG-GAAGAAGGCAGTGCCCAGCTCCTG3'. The method used was that of Bensi et al [38]. In brief, 0.2 pmol 5'-32P-labeled oligonucleotide were mixed with 1-2 pg Me2SO-denatured liver polyadenylated RNA in a 50 mM Tris/HCI buffer (PH 8.3), 8 mM MgC12, 50mM KCI, 0.4mM dithiothreitol, 1 mM dNTPs.…”

Section: Primer Extension Analysismentioning

confidence: 99%

Tissue‐specific heterogeneity of the 3′‐untranslated region of L‐type pyruvate kinase mRNAs

Marie¹,

Simon²,

Lone³

et al. 1986

European Journal of Biochemistry

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A single L-type pyruvate kinase (PK) gene seems to exist per haploid genome. It is expressed in the liver, kidney and small intestine in the form of three mRNA species of 2, 2.2 and 3.2 x l o 3 bases (kb). All three species are polyadenylated and translatable into the same L-type subunit. Primer extension experiments demonstrate that all three PK mRNAs have the same 5' ends. Nuclease S1 protection experiments with various cDNA and 3' genomic probes indicate that the different mRNA species only differ by the length of their 3' noncoding region. The mechanism responsible for the production of the three transcripts seems to be the use of alternative unusual polyadenylation sites. Run-on assays with specific probes recognizing only the 3.2-kb or all three mRNA species show that the transcription proceeds across the gene with similar rate. This means that the process involved in generation of the three transcripts is a posttranscriptional event, probably due to different sites of endonucleolytic cleavage of primary transcripts extending 3' from the gene region encoding the mature mRNAs. The ratio between the different PK mRNA species is, to a certain extent, tissue-specific and changes with development. The role of an 'identifier sequence' located in the 3' noncoding sequence of the 3.2-kb species in such a tissue-specific use of alternative polyadenylation sites is discussed.Many strategies are used by eucaryotic genes to modulate their expression. Accumulating evidence suggests that RNA processing is one of the biochemical events frequently involved in regulation of gene expression. In fact, several processes can be responsible for the production of different messenger RNAs from the same gene. Multiple RNAs could be generated from primary transcripts whose synthesis is controlled by alternative promotors, this phenomenon being then associated with differential splicing events [l -51.These RNAs could be derived from the same primary transcript through differential splicing events or selective choice of several polyadenylation sites eventually coupled with alternative splicing phenomena [6 -231. These alternative RNA processing events sometimes exhibit tissue and developmental specificity [5, 8, 11, 15, 18, 191. We have recently isolated liver L-type pyruvate kinase (PK) cDNA clones and used them to analyze RNAs from different tissues. Three mRNA species of 3.2, 2.2 and 2 kb were found in liver and in tissues which express L-type PK [24,25]. Genetic arguments, Southern blot analysis and detection of a single type of PK genomic clone in a rat DNA library demonstrate that they are encoded by the same gene.We show here that these different messenger RNAs share identical noncoding 5' and coding regions and differ only by the length of their 3' untranslated extensions, probably through the use of alternative polyadenylation sites. Moreover Abbreviations. kb, lo3 bases; SDS, sodium dodecyl sulphate; PK, pyruvate kinase.Enzyme. Pyruvate kinase (EC 2.7.1.40).the three different RNAs are expressed in a relatively tissuespec...

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Structure and expression of the human haptoglobin locus.

Cited by 147 publications

References 22 publications

Complete nucleotide and deduced amino acid sequences of rat L‐type pyruvate kinase

Complete nucleotide and deduced amino acid sequences of rat L‐type pyruvate kinase

A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family.

Tissue‐specific heterogeneity of the 3′‐untranslated region of L‐type pyruvate kinase mRNAs

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