193 research outputs found
Epistasis not needed to explain low dN/dS
An important question in molecular evolution is whether an amino acid that
occurs at a given position makes an independent contribution to fitness, or
whether its effect depends on the state of other loci in the organism's genome,
a phenomenon known as epistasis. In a recent letter to Nature, Breen et al.
(2012) argued that epistasis must be "pervasive throughout protein evolution"
because the observed ratio between the per-site rates of non-synonymous and
synonymous substitutions (dN/dS) is much lower than would be expected in the
absence of epistasis. However, when calculating the expected dN/dS ratio in the
absence of epistasis, Breen et al. assumed that all amino acids observed in a
protein alignment at any particular position have equal fitness. Here, we relax
this unrealistic assumption and show that any dN/dS value can in principle be
achieved at a site, without epistasis. Furthermore, for all nuclear and
chloroplast genes in the Breen et al. dataset, we show that the observed dN/dS
values and the observed patterns of amino acid diversity at each site are
jointly consistent with a non-epistatic model of protein evolution.Comment: This manuscript is in response to "Epistasis as the primary factor in
molecular evolution" by Breen et al. Nature 490, 535-538 (2012
Cryptic t(19;19)(p13.3;q13.2), involving the TCF3/E2A gene, detected and described by molecular cytogenetics in a patient with childhood B-cell progenitor acute lymphoblastic leukemia
Case report on a case of cryptic t(19;19)(p13.3;q13.2), involving the TCF3/E2A gene, detected and described by molecular cytogenetics in a patient with childhood B-cell progenitor acute lymphoblastic leukemia
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