Evolution of the Adh locus in the Drosophila willistoni group: the loss of an intron, and shift in codon usage.

Anderson, Cort L.; Carew, Elizabeth; Powell, Jeffrey R.

doi:10.1093/oxfordjournals.molbev.a040027

Cited by 22 publications

(1 citation statement)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Data from multiple species have found that the choice of synonymous codons can impact fitness, differing in the speed and accuracy with which they are read as a consequence of tRNA abundance and modification. In this regard, it is interesting that a dramatic shift in codon preference has been identified across the drosophilid lineage and in particular for the amino acids tyrosine, histidine, asparagine and aspartic acid [ 149 , 150 , 151 , 152 ]. For example, D. melanogaster show a preference for NAC codons whereas D. virilis has a preference for NAU codons [ 153 ].…”

Section: Queuosine In Translationmentioning

confidence: 99%

The Queuine Micronutrient: Charting a Course from Microbe to Man

et al. 2015

View full text Add to dashboard Cite

Micronutrients from the diet and gut microbiota are essential to human health and wellbeing. Arguably, among the most intriguing and enigmatic of these micronutrients is queuine, an elaborate 7-deazaguanine derivative made exclusively by eubacteria and salvaged by animal, plant and fungal species. In eubacteria and eukaryotes, queuine is found as the sugar nucleotide queuosine within the anticodon loop of transfer RNA isoacceptors for the amino acids tyrosine, asparagine, aspartic acid and histidine. The physiological requirement for the ancient queuine molecule and queuosine modified transfer RNA has been the subject of varied scientific interrogations for over four decades, establishing relationships to development, proliferation, metabolism, cancer, and tyrosine biosynthesis in eukaryotes and to invasion and proliferation in pathogenic bacteria, in addition to ribosomal frameshifting in viruses. These varied effects may be rationalized by an important, if ill-defined, contribution to protein translation or may manifest from other presently unidentified mechanisms. This article will examine the current understanding of queuine uptake, tRNA incorporation and salvage by eukaryotic organisms and consider some of the physiological consequence arising from deficiency in this elusive and lesser-recognized micronutrient.

show abstract

Section: Queuosine In Translationmentioning

confidence: 99%

The Queuine Micronutrient: Charting a Course from Microbe to Man

et al. 2015

View full text Add to dashboard Cite

show abstract

ADH evolution and the phylogenetic footprint

Dorit

Ayala

1995

J Mol Evol

View full text Add to dashboard Cite

The evolution of any given protein reflects the interplay between proximal selective forces involving the conservation of protein structure and function and more general populational factors that shape the action and efficiency of natural selection. In an attempt to address that interplay, we have analyzed patterns of amino acid replacement within a well-conserved molecule, alcohol dehydrogenase (ADH), in the Drosophilidae. A sliding window, moved along the protein sequence in order to quantify the extent of change at each amino acid position, reveals heterogeneous amounts of replacement across the molecule when all ADH sequences are analyzed simultaneously. Surprisingly, the replacement profile for ADH differs significantly in the melanogaster, mulleri, and Hawaiian subgroups, reflecting the imprint of the differing evolutionary histories of each of these assemblages on the evolution of this conservative molecule.

show abstract

Molecular evolution of thepaired gene inDrosophila: Cloning and characterization of the partialpaired gene fromDrosophila willistoni

Matsuo

1996

Biochem Genet

View full text Add to dashboard Cite

A partial paired gene of Drosophila willistoni containing the paired box and extended homeo box was amplified by PCR and the nucleotide sequence of 1141 bp was determined. Comparison of the paired genes in D. willistoni and D. melanogaster showed that the proportions of identical nucleotide sites in the coding region and identical amino acid sites were 73.8 and 86.5%, respectively. The amino acid sites in the N-terminal region, the paired box, and the extended homeo box were 88.5, 95.3, and 98.6% identical in the two species. The rates of amino acid substitution for these regions were estimated to be 1.73 x 10(-9), 0.67 x 10(-9), and 0.19 x 10(-9)/site/year, respectively. In contrast, the connecting region between the two boxes has been highly diverged and evolved very rapidly, 18.3 x 10(-9)/site/year, suggesting almost no functional constraint in the connecting region.

show abstract

Evolution of the Adh locus in the Drosophila willistoni group: the loss of an intron, and shift in codon usage.

Cited by 22 publications

References 27 publications

The Queuine Micronutrient: Charting a Course from Microbe to Man

The Queuine Micronutrient: Charting a Course from Microbe to Man

ADH evolution and the phylogenetic footprint

Molecular evolution of thepaired gene inDrosophila: Cloning and characterization of the partialpaired gene fromDrosophila willistoni

Contact Info

Product

Resources

About