Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2008-9-10
pubmed:databankReference
pubmed:abstractText
Vertebrate ancestors appeared in a uniform, shallow water environment, but modern species flourish in highly variable niches. A striking array of phenotypes exhibited by contemporary animals is assumed to have evolved by accumulating a series of selectively advantageous mutations. However, the experimental test of such adaptive events at the molecular level is remarkably difficult. One testable phenotype, dim-light vision, is mediated by rhodopsins. Here, we engineered 11 ancestral rhodopsins and show that those in early ancestors absorbed light maximally (lambda(max)) at 500 nm, from which contemporary rhodopsins with variable lambda(max)s of 480-525 nm evolved on at least 18 separate occasions. These highly environment-specific adaptations seem to have occurred largely by amino acid replacements at 12 sites, and most of those at the remaining 191 ( approximately 94%) sites have undergone neutral evolution. The comparison between these results and those inferred by commonly-used parsimony and Bayesian methods demonstrates that statistical tests of positive selection can be misleading without experimental support and that the molecular basis of spectral tuning in rhodopsins should be elucidated by mutagenesis analyses using ancestral pigments.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-10339578, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-10512613, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-10736710, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-10785616, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-10926528, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-11448887, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-11573008, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-12200476, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-12618404, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-12824471, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15014169, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15269277, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15327956, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15653464, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15689528, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15772376, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15781694, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-15809435, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-16756510, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-16767103, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-16922606, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-17483113, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-17498892, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-17703238, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-18768803, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-4424870, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-8185948, http://linkedlifedata.com/resource/pubmed/commentcorrection/18768804-9442898
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1091-6490
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13480-5
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Elucidation of phenotypic adaptations: Molecular analyses of dim-light vision proteins in vertebrates.
pubmed:affiliation
Department of Biology, Emory University, Atlanta, GA 30322, USA. syokoya@emory.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural