| dc.contributor.author |
Arhontaki, K |
en |
| dc.contributor.author |
Eliopoulos, E |
en |
| dc.contributor.author |
Goulielmos, G |
en |
| dc.contributor.author |
Kastanis, P |
en |
| dc.contributor.author |
Tsakas, S |
en |
| dc.contributor.author |
Loukas, M |
en |
| dc.contributor.author |
Ayala, F |
en |
| dc.date.accessioned |
2014-06-06T06:45:03Z |
|
| dc.date.available |
2014-06-06T06:45:03Z |
|
| dc.date.issued |
2002 |
en |
| dc.identifier.issn |
00222844 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1007/s00239-002-2370-9 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/2223 |
|
| dc.subject |
3D structure |
en |
| dc.subject |
Amino acid sequence |
en |
| dc.subject |
Cu,Zn SOD |
en |
| dc.subject |
Drosophila melanogaster subgroup |
en |
| dc.subject |
Phylogeny |
en |
| dc.subject.other |
copper zinc superoxide dismutase |
en |
| dc.subject.other |
genomic DNA |
en |
| dc.subject.other |
DNA |
en |
| dc.subject.other |
superoxide dismutase |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
Drosophila melanogaster |
en |
| dc.subject.other |
molecular cloning |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
nucleotide sequence |
en |
| dc.subject.other |
phylogeny |
en |
| dc.subject.other |
polymerase chain reaction |
en |
| dc.subject.other |
species difference |
en |
| dc.subject.other |
amino acid sequence |
en |
| dc.subject.other |
animal |
en |
| dc.subject.other |
enzymology |
en |
| dc.subject.other |
genetics |
en |
| dc.subject.other |
metabolism |
en |
| dc.subject.other |
molecular genetics |
en |
| dc.subject.other |
sequence homology |
en |
| dc.subject.other |
Bos taurus |
en |
| dc.subject.other |
Drosophila melanogaster |
en |
| dc.subject.other |
Melanogaster |
en |
| dc.subject.other |
Xenopus laevis |
en |
| dc.subject.other |
Amino Acid Sequence |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Base Sequence |
en |
| dc.subject.other |
DNA |
en |
| dc.subject.other |
Drosophila melanogaster |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Phylogeny |
en |
| dc.subject.other |
Sequence Homology, Amino Acid |
en |
| dc.subject.other |
Species Specificity |
en |
| dc.subject.other |
Superoxide Dismutase |
en |
| dc.title |
Functional constraints of the Cu,Zn superoxide dismutase in species of the Drosophila melanogaster subgroup and phylogenetic analysis |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1007/s00239-002-2370-9 |
en |
| heal.publicationDate |
2002 |
en |
| heal.abstract |
The phylogenetic relationships among the Drosophila melanogaster subgroup species were analyzed using approximately 1550-nucleotide-long sequences of the Cu,Zn SOD gene. Phylogenetic analysis was performed using separately the whole region and the intron sequences of the gene. The resulting phylogenetic trees reveal virtually the same topology, separating the species into distinct clusters. The inferred topology generally agrees with previously proposed classifications based on morphological and molecular data. The amino acid sequences of the Cu,Zn SOD of the D. melanogaster subgroup species reveal a high-conservation pattern. Only 3.9% of the total amino acid sites are variable, and none affects the major structural elements. Comparison of the Drosophila Cu,Zn SOD amino acid sequences with the Cu,Zn SOD of Bos taurus and Xenopus laevis (whose three-dimensional structure has been elucidated) reveals conservation of all the protein's functionally important amino acids and no substitutions that dramatically change the charge or the polarity of the amino acids. |
en |
| heal.journalName |
Journal of Molecular Evolution |
en |
| dc.identifier.issue |
6 |
en |
| dc.identifier.volume |
55 |
en |
| dc.identifier.doi |
10.1007/s00239-002-2370-9 |
en |
| dc.identifier.spage |
745 |
en |
| dc.identifier.epage |
756 |
en |