Chromosome mapping of the genes for murine arylamine N-acetyltransferases (NATs), enzymes involved in the metabolism of carcinogens: identification of a novel upstream noncoding exon for murine Nat2

2000 ◽  
Vol 90 (1-2) ◽  
pp. 134-138 ◽  
Author(s):  
G. Fakis ◽  
S. Boukouvala ◽  
V. Buckle ◽  
M. Payton ◽  
C. Denning ◽  
...  
Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 826
Author(s):  
Rafael Kretschmer ◽  
Marcelo Santos de Souza ◽  
Ivanete de Oliveira Furo ◽  
Michael N. Romanov ◽  
Ricardo José Gunski ◽  
...  

Interchromosomal rearrangements involving microchromosomes are rare events in birds. To date, they have been found mostly in Psittaciformes, Falconiformes, and Cuculiformes, although only a few orders have been analyzed. Hence, cytogenomic studies focusing on microchromosomes in species belonging to different bird orders are essential to shed more light on the avian chromosome and karyotype evolution. Based on this, we performed a comparative chromosome mapping for chicken microchromosomes 10 to 28 using interspecies BAC-based FISH hybridization in five species, representing four Neoaves orders (Caprimulgiformes, Piciformes, Suliformes, and Trogoniformes). Our results suggest that the ancestral microchromosomal syntenies are conserved in Pteroglossus inscriptus (Piciformes), Ramphastos tucanus tucanus (Piciformes), and Trogon surrucura surrucura (Trogoniformes). On the other hand, chromosome reorganization in Phalacrocorax brasilianus (Suliformes) and Hydropsalis torquata (Caprimulgiformes) included fusions involving both macro- and microchromosomes. Fissions in macrochromosomes were observed in P. brasilianus and H. torquata. Relevant hypothetical Neognathae and Neoaves ancestral karyotypes were reconstructed to trace these rearrangements. We found no interchromosomal rearrangement involving microchromosomes to be shared between avian orders where rearrangements were detected. Our findings suggest that convergent evolution involving microchromosomal change is a rare event in birds and may be appropriate in cytotaxonomic inferences in orders where these rearrangements occurred.


Genetics ◽  
1960 ◽  
Vol 45 (8) ◽  
pp. 1085-1110 ◽  
Author(s):  
D C Hawthorne ◽  
R K Mortimer
Keyword(s):  

Genome ◽  
2002 ◽  
Vol 45 (4) ◽  
pp. 661-669 ◽  
Author(s):  
Ali Masoudi-Nejad ◽  
Shuhei Nasuda ◽  
Akira Kawabe ◽  
Takashi R Endo

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the α-, β-, γ-, and ω-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an ω-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the ω-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the ω-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the α- and β-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the ω-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The ω-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the ω-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-A1a in 'Chinese Spring'.Key words: glutenin, omega gliadin, storage protein, Triticum aestivum, secalin.


2014 ◽  
Vol 37 (1) ◽  
pp. 46-53 ◽  
Author(s):  
Leila Braga Ribeiro ◽  
Daniele Aparecida Matoso ◽  
Eliana Feldberg

Gene ◽  
2002 ◽  
Vol 292 (1-2) ◽  
pp. 167-171 ◽  
Author(s):  
Irene Marcos ◽  
Salud Borrego ◽  
Santiago Rodrı́guez de Córdoba ◽  
José Jorge Galán ◽  
Guillermo Antiñolo
Keyword(s):  

1995 ◽  
Author(s):  
B.L. Marrone ◽  
L.L. Deaven ◽  
D.J. Chen ◽  
Min S. Park ◽  
M.A. MacInnes ◽  
...  

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