Assignment of the human and mouse prion protein genes to homologous chromosomes.

Sparkes, Robert S.; Simon, M; Cohn, Vivian H.; Fournier, R. E. K.; Lem, Janis; Klisak, I; Heinzmann, C.; Blatt, Cila; Lucero, Miguel A.; Mohandas, T.

doi:10.1073/pnas.83.19.7358

Cited by 192 publications

(70 citation statements)

References 36 publications

(36 reference statements)

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“…A study on the correlation between the murine prion protein sequence and length of scrapie incubation period suggested that the Prn-i gene was linked to or congruent with the murine prion protein gene (Prn-p) which encoded the prion protein. These genes from the prion gene complex were located on chromosome 2 (Sparkes et al, 1986). Studies of the nucleotide sequence of the Prn-p gene of inbred mouse strains revealed substitutions at codons 108 and 189 (Westaway et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Host Genetic Control of Incubation Periods of Creutzfeldt-Jakob Disease in Mice

Mohri

Tateishi

1989

Journal of General Virology

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SUMMARYHost genetic control of the incubation period of Creutzfeldt-Jakob disease (CJD) was studied using various inbred strains of mice, including B10 congenic strains. Various incubation periods were found in mice injected either intracerebrally or intraperitoneally with the Fukuoka 1 strain of the CJD agent; NZW/Sea and A/JJms had the shortest, and BI0.AKM/OIa and C57BL/6J the longest, incubation periods. Length of the CJD incubation period did not correlate with the genetic markers tested, i.e. the murine major histocompatibility (H-2) complex (which has previously been reported to be linked to a gene influencing CJD incubation period in mice), coat colour or sex genes. In NZW/Sea × C57BL/6J F 1 hybrid mice the CJD incubation periods were similar to that of the parent with the longest incubation period. Incubation periods of the backcross progeny from F1 and NZW/Sea were intermediate between those of the parental mice and had a unimodal distribution pattern. A similar observation was made on the progeny of the A/JJms x C57BL/6J mating. On the other hand, the length of incubation period for the NZW/Sea x B10. AKM/Ola F1 hybrid fell between those for the two parents and the NZW/Sea x A/JJms F~ hybrid had a significantly longer incubation period than those of the two parents. These results suggest that polygenes probably control the length of the CJD incubation period in mice.

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Section: Introductionmentioning

confidence: 99%

Host Genetic Control of Incubation Periods of Creutzfeldt-Jakob Disease in Mice

Mohri

Tateishi

1989

Journal of General Virology

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“…The presence of the human and mouse PrP genes within conserved syntenic groups (Sparkes et al 1986) and the presence of a PrP gene in chicken (Gabriel et al 1992) argue that the PrP gene existed before the speciation of mammals. In mammals, DNA sequences of the ORFs encoding PrP generally exhibit ∼90% similarity.…”

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confidence: 99%

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Lee

Westaway²,

Smit³

et al. 1998

Genome Res.

155

125

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The prion protein (PrP), first identified in scrapie-infected rodents, is encoded by a single exon of a single-copy chromosomal gene. In addition to the protein-coding exon, PrP genes in mammals contain one or two 5′-noncoding exons. To learn more about the genomic organization of regions surrounding the PrP exons, we sequenced 105 bp of DNA from clones containing human, sheep, and mouse PrP genes isolated in cosmids or λ phage. Our findings are as follows: (1) Although the human PrP transcript does not include the untranslated exon 2 found in its mouse and sheep counterparts, the large intron of the human PrP gene contains an exon 2-like sequence flanked by consensus splice acceptor and donor sites. (2) The mouse Prnpa but not thePrnpb allele found in 44 inbred lines contains a 6593 nucleotide retroviral genome inserted into the anticoding strand of intron 2. This intracisternal A-particle element is flanked by duplications of an AAGGCT nucleotide motif. (3) We found that thePrP gene regions contain from 40% to 57% genome-wide repetitive elements that independently increased the size of the locus in all three species by numerous mutations. The unusually long sheepPrP 3′-untranslated region contains a “fossil” 1.2-kb mariner transposable element. (4) We identified sequences in noncoding DNA that are conserved between the three species and may represent biologically functional sites.[The nucleotide sequence data reported in this paper have been submitted to the GenBank sequence database and have been assigned the accession numbers U29185(human), U29186 (mouse), and U67922 (sheep).]

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“…These GϩC nonamers represent a motif that may function as a canonical binding site for the transcription factor Sp1 (203). Mapping of PrP genes to the short arm of Hu chromosome 20 and to the homologous region of Mo chromosome 2 argues for the existence of PrP genes prior to the speciation of mammals (204,205).…”

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confidence: 99%

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

Chisholm

Dahlbeck

Krishnamurthy

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

137

138

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Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP). Bovine spongiform encephalopathy (BSE), scrapie of sheep, and Creutzfeldt-Jakob disease (CJD) of humans are among the most notable prion diseases. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrP Sc ). The normal, cellular PrP (PrP C ) is converted into PrP Sc through a posttranslational process during which it acquires a high ␤-sheet content. The species of a particular prion is encoded by the sequence of the chromosomal PrP gene of the mammals in which it last replicated. In contrast to pathogens carrying a nucleic acid genome, prions appear to encipher strain-specific properties in the tertiary structure of PrP Sc . Transgenetic studies argue that PrP Sc acts as a template upon which PrP C is refolded into a nascent PrP Sc molecule through a process facilitated by another protein. Miniprions generated in transgenic mice expressing PrP, in which nearly half of the residues were deleted, exhibit unique biological properties and should facilitate structural studies of PrP Sc . While knowledge about prions has profound implications for studies of the structural plasticity of proteins, investigations of prion diseases suggest that new strategies for the prevention and treatment of these disorders may also find application in the more common degenerative diseases.

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Assignment of the human and mouse prion protein genes to homologous chromosomes.

Cited by 192 publications

References 36 publications

Host Genetic Control of Incubation Periods of Creutzfeldt-Jakob Disease in Mice

Host Genetic Control of Incubation Periods of Creutzfeldt-Jakob Disease in Mice

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

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