Consideration of the evolution of theSaccharomyces cerevisiae MEL gene family on the basis of the nucleotide sequences of the genes and their flanking regions

Yeast ◽  
1994 ◽  
Vol 10 (12) ◽  
pp. 1559-1568 ◽  
Author(s):  
Hilkka Turakainen ◽  
Paula Kristo ◽  
Matti Korhola
1987 ◽  
Vol 7 (5) ◽  
pp. 1938-1946
Author(s):  
K Shahan ◽  
M Gilmartin ◽  
E Derman

The mouse major urinary proteins (MUPs) are encoded by a gene family of about 35 to 40 members. MUPs are synthesized in at least six secretory tissues under a variety of developmental and endocrine controls, but the identities of the individual genes expressed in each tissue have not previously been established. In this article, we present the nucleotide sequences of five MUP mRNAs which we designate MUP I through V. MUPs I, II, and III are the most abundant MUP mRNA species in the liver, and MUPs IV and V are the most abundant MUP mRNA species in the lachrymal gland and the submaxillary gland, respectively. The sequence data show that each of the five mRNAs is encoded by a distinct member of the gene family. The structures of the MUP mRNA consist of interspersed segments of variable and conserved sequences. On the basis of the sequences of the variable segments, gene-specific panels of synthetic oligonucleotide probes were prepared. The gene-specific panels were used to identify cloned genes and, as described in the accompanying paper (K. Shahan, M. Denaro, M. Gilmartin, Y. Shi, and E. Derman, Mol. Cell. Biol. 7:1947-1954, 1987), to characterize the expression of MUP genes I through V.


2013 ◽  
Vol 58 (No. 2) ◽  
pp. 79-90 ◽  
Author(s):  
A. Van den Broeke ◽  
M. Van Poucke ◽  
A. Van Zeveren ◽  
L.J. Peelman

The ribosomal protein SA (RPSA), also known as 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR), has been identified as a multifunctional protein, playing an important role in multiple pathologies like cancer and prion diseases. Since RPSA is involved in the binding and internalization of the prion protein, mutations in the ovine RPSA gene, influencing the RPSA-PrP<sup>C</sup>/PrP<sup>Sc </sup>binding, can potentially play a part in the resistance to prion diseases. Our goal was to further characterize the complex RPSA gene family and to detect structural mutations which can play a role in this disease. In a prior study, 11 ovine pseudogenes were detected experimentally. As the whole genome shotgun ovine genome became accessible, an in silico genome-wide screening was performed and 37 new pseudogenes (36 processed and one semi-processed pseudogene) were detected, bringing the total to 48 ovine RPSA pseudogenes. Additionally, the complete bovine genome was screened in silico and 56 pseudogenes were identified. Once these sequences were known, it was possible to analyze the presence of mutations in the coding sequence and exon-flanking regions of the ovine functional full-length RPSA gene without the interference of pseudogenic sequences. Nineteen mutations were found: one in the 5&rsquo; UTR, a silent one in the coding region, and seventeen in the exon-flanking regions, including an interesting mutation in the SNORA62 gene, localized in intron 4 of RPSA, leading to potential ribosomal defects. Structural mutations of the RPSA gene can be ruled out to play a role in transmissible spongiform encephalopathies but regulatory mutations still can have an effect on these diseases.


Gene ◽  
1991 ◽  
Vol 108 (2) ◽  
pp. 311-312 ◽  
Author(s):  
T. Nakayama ◽  
S. Takechi ◽  
T. Ohshige ◽  
K. Kondo ◽  
K. Yamamoto

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Anatoliy T. Ivashchenko ◽  
Assel S. Issabekova ◽  
Olga A. Berillo

OnlyPTPN12, MSH6, andZEB1have significant miR-1279 binding sites among paralogous genes of human tyrosine phosphatase family, DNA mismatch repair family, and zinc finger family, respectively. All miRNA binding sites are located within CDSs of studied mRNAs. Nucleotide sequences of hsa-miR-1279 binding sites with mRNAs of humanPTPN12, MSH6, andZEB1genes encode TKEQYE, EGSSDE, and GEKPYE oligopeptides, respectively. The conservation of miRNA binding sites encoding oligopeptides has been revealed. MRNAs of many paralogs of zinc finger gene family have from 1 to 12 binding sites coding the same GEKPYE hexapeptide. MRNAs ofPTPN12, MSH6, andZEB1orthologous genes from different animal species have binding sites for hsa-miR-1279 which consist of homologous oligonucleotides encoding similar human oligopeptides TKEQYE, EGSSDE, and GEKPYE. MiR-548j, miR-548m, and miR-548d-5p have homologous binding sites in the mRNA ofPTPN12orthologous genes which encode PRTRSC, TEATDI, and STASAT oligopeptides, respectively. All regions of miRNA are important for binding with the mRNA.


1985 ◽  
Vol 5 (6) ◽  
pp. 1343-1348 ◽  
Author(s):  
D Le Roscouet ◽  
G Vodjdani ◽  
Y Lemaigre-Dubreuil ◽  
M G Tovey ◽  
M Latta ◽  
...  

A murine alpha interferon pseudogene was identified in a mouse genomic library. The nucleotide sequence revealed several in-phase termination codons within the gene and repetitive oligonucleotides in the flanking regions. The nucleotide sequences and the amino acids of the peptide signal sequences were compared with known human alpha interferon genes and the pseudogene.


1998 ◽  
Vol 79 (01) ◽  
pp. 150-154 ◽  
Author(s):  
Masafumi Kida ◽  
Masuyo H.- Kawabata ◽  
Tomio Yamazaki ◽  
Akitada Ichinose

SummaryWhen we compared nucleotide sequences of the 5’-flanking regions for plasminogen genes from 11 individuals, six substitutions were identified even among normal subjects. A new haplotype (termed allele II) was screened by PCR-RFLP analysis among 54 Japanese and 58 Caucasian normal subjects. The frequency of allele II was 0.787 in the Japanese and 0.560 in the Caucasians, indicating that the ratio of alleles differs between populations. Examination of 118 cases with dysplasminogenemia revealed that the Ala601-Thr mutation was present on allele I in most cases. This mutation was also associated with allele II in one-fourth of all cases, suggesting possible recombination within the plasminogen gene. Interestingly, we previously demonstrated that the expression activity of allele II was about 1.8 fold that of allele I in vitro.


1987 ◽  
Vol 7 (5) ◽  
pp. 1938-1946 ◽  
Author(s):  
K Shahan ◽  
M Gilmartin ◽  
E Derman

The mouse major urinary proteins (MUPs) are encoded by a gene family of about 35 to 40 members. MUPs are synthesized in at least six secretory tissues under a variety of developmental and endocrine controls, but the identities of the individual genes expressed in each tissue have not previously been established. In this article, we present the nucleotide sequences of five MUP mRNAs which we designate MUP I through V. MUPs I, II, and III are the most abundant MUP mRNA species in the liver, and MUPs IV and V are the most abundant MUP mRNA species in the lachrymal gland and the submaxillary gland, respectively. The sequence data show that each of the five mRNAs is encoded by a distinct member of the gene family. The structures of the MUP mRNA consist of interspersed segments of variable and conserved sequences. On the basis of the sequences of the variable segments, gene-specific panels of synthetic oligonucleotide probes were prepared. The gene-specific panels were used to identify cloned genes and, as described in the accompanying paper (K. Shahan, M. Denaro, M. Gilmartin, Y. Shi, and E. Derman, Mol. Cell. Biol. 7:1947-1954, 1987), to characterize the expression of MUP genes I through V.


1994 ◽  
Vol 31 (1) ◽  
pp. 79-82 ◽  
Author(s):  
X.X. Tang ◽  
N. Ikegaki ◽  
E. Heber-Katz

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