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1.
BMC Genet ; 10: 86, 2009 Dec 20.
Article in English | MEDLINE | ID: mdl-20021697

ABSTRACT

BACKGROUND: The chicken (Gallus gallus), like most avian species, has a very distinct karyotype consisting of many micro- and a few macrochromosomes. While it is known that recombination frequencies are much higher for micro- as compared to macrochromosomes, there is limited information on differences in linkage disequilibrium (LD) and haplotype diversity between these two classes of chromosomes. In this study, LD and haplotype diversity were systematically characterized in 371 birds from eight chicken populations (commercial lines, fancy breeds, and red jungle fowl) across macro- and microchromosomes. To this end we sampled four regions of approximately 1 cM each on macrochromosomes (GGA1 and GGA2), and four 1.5 -2 cM regions on microchromosomes (GGA26 and GGA27) at a high density of 1 SNP every 2 kb (total of 889 SNPs). RESULTS: At a similar physical distance, LD, haplotype homozygosity, haploblock structure, and haplotype sharing were all lower for the micro- as compared to the macrochromosomes. These differences were consistent across populations. Heterozygosity, genetic differentiation, and derived allele frequencies were also higher for the microchromosomes. Differences in LD, haplotype variation, and haplotype sharing between populations were largely in line with known demographic history of the commercial chicken. Despite very low levels of LD, as measured by r2 for most populations, some haploblock structure was observed, particularly in the macrochromosomes, but the haploblock sizes were typically less than 10 kb. CONCLUSION: Differences in LD between micro- and macrochromosomes were almost completely explained by differences in recombination rate. Differences in haplotype diversity and haplotype sharing between micro- and macrochromosomes were explained by differences in recombination rate and genotype variation. Haploblock structure was consistent with demography of the chicken populations, and differences in recombination rates between micro- and macrochromosomes. The limited haploblock structure and LD suggests that future whole-genome marker assays will need 100+K SNPs to exploit haplotype information. Interpretation and transferability of genetic parameters will need to take into account the size of chromosomes in chicken, and, since most birds have microchromosomes, in other avian species as well.


Subject(s)
Chickens/genetics , Chromosome Mapping , Haplotypes , Linkage Disequilibrium , Animals , Female , Gene Frequency , Genetics, Population , Male , Polymorphism, Single Nucleotide , Sequence Analysis, DNA
2.
Appl Environ Microbiol ; 74(15): 4671-9, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18539791

ABSTRACT

When Lactococcus lactis subsp. lactis IL1403 or L. lactis subsp. cremoris MG1363 is grown in a medium with galactose as the carbon source, the culture lyses to a lesser extent in stationary phase than when the bacteria are grown in a medium containing glucose. Expression of AcmA, the major autolysin of L. lactis, is not influenced by the carbon source. Binding studies with a fusion protein consisting of the MSA2 protein of Plasmodium falciparum and the C-terminal peptidoglycan-binding domain of AcmA revealed that cell walls of cells from both subspecies grown on galactose bind less AcmA than cell walls of cells grown on glucose. Cells grown on glucose or galactose and treated with trichloroacetic acid prior to AcmA binding bind similar amounts of AcmA. Analysis of the composition of the lipoteichoic acids (LTAs) of L. lactis IL1403 cells grown on glucose or galactose showed that the LTA composition is influenced by the carbon source: cells grown on galactose contain LTA with less galactose than cells grown on glucose. In conclusion, growth of L. lactis on galactose changes the LTA composition in the cell wall in such a way that less AcmA is able to bind to the peptidoglycan, resulting in a decrease in autolysis.


Subject(s)
Cell Wall/physiology , Galactose/metabolism , Lactococcus lactis/physiology , Muramidase/metabolism , Autolysis , Bacteriolysis , Base Sequence , Cell Wall/drug effects , DNA, Bacterial/genetics , Kinetics , Lactococcus lactis/genetics , Lactococcus lactis/growth & development , Molecular Sequence Data , Peptidoglycan/metabolism , Plasmids/genetics , Protein Binding , Restriction Mapping
3.
Mol Genet Genomics ; 273(4): 319-25, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15812650

ABSTRACT

We have cloned the Aspergillus niger dapB gene. Analysis of its nucleotide sequence and the corresponding protein sequence indicates that the gene encodes a type IV dipeptidyl aminopeptidase (DPP IV). Based upon its deduced sequence we predict the presence of a transmembrane domain in the protein. Furthermore, dapB-overexpressing transformants display an increase in intracellular DPP IV activity. This is the first reported characterisation of a dipeptidyl aminopeptidase with a transmembrane domain from a filamentous fungus. Using the dapB sequence as a query, we were able to identify 14 DPP IV-encoding genes, and 12 additional DPPIV proteases in public genomic databases. Phylogenetic analysis reveals that in yeasts there are two clades of genes that encode DPP IV proteases with a transmembrane domain. In this study we demonstrate that, as in yeasts, two classes of DPP IV-encoding genes exist in filamentous fungi. However, only one of these codes for DPP IV proteases with a transmembrane domain. The second type present in filamentous fungi encodes extracellular DPP IV proteases. The dapB gene belongs to the first cluster. We propose that DapB plays a role in the proteolytic maturation of enzymes produced by A. niger.


Subject(s)
Aspergillus niger/genetics , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/genetics , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/metabolism , Genes, Fungal/genetics , Membrane Proteins/genetics , Phylogeny , Aspergillus niger/enzymology , Base Sequence , Blotting, Northern , Blotting, Southern , Cluster Analysis , Computational Biology , DNA Primers , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/classification , Molecular Sequence Data , Protein Structure, Tertiary , Sequence Analysis, DNA
4.
Blood Cells Mol Dis ; 34(2): 151-6, 2005.
Article in English | MEDLINE | ID: mdl-15727898

ABSTRACT

Hereditary hemochromatosis (HH) is a frequent genetic disease of older subjects of northern European descent. It is characterized by increased iron absorption and severe iron overloading in parenchymal organs. A similar disturbance of iron metabolism occurs in specific animal species in captivity. To address the key features leading to high absorption and thus to iron overload in these animals, we have studied the two iron transport proteins DMT1 and Ireg1 in the best-known susceptible species, the mynah bird. Here, we show that these birds have a high expression of DMT1 in the duodenum and also a strikingly high expression of Ireg1 along the whole small intestine. We believe that the iron accumulation in susceptible species only occurs in captivity because of a genotypic adaptation to their natural environment, where contrary to captivity, dietary iron is hardly available. The Caucasian population carrying mutations leading to iron overload today may have also benefited from the genetic advantage of up-regulating iron transport millennia ago, when dietary iron was scarce.


Subject(s)
Iron/metabolism , Liver/metabolism , Amino Acid Sequence , Animals , Base Sequence , Cation Transport Proteins/genetics , Cation Transport Proteins/metabolism , Chickens , DNA Primers , Expressed Sequence Tags , Humans , Intestine, Small/cytology , Intestine, Small/metabolism , Iron-Binding Proteins/genetics , Iron-Binding Proteins/metabolism , Kidney/cytology , Kidney/metabolism , Liver/cytology , Molecular Sequence Data , Polymerase Chain Reaction , Sequence Alignment , Sequence Homology, Amino Acid , Starlings
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