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dc.contributor.authorHietpas, Ryan T.
dc.contributor.authorJensen, Jeffrey D.
dc.contributor.authorBolon, Daniel N. A.
dc.date2022-08-11T08:08:55.000
dc.date.accessioned2022-08-23T16:12:01Z
dc.date.available2022-08-23T16:12:01Z
dc.date.issued2011-05-10
dc.date.submitted2013-09-24
dc.identifier.citation<p>Proc Natl Acad Sci U S A. 2011 May 10;108(19):7896-901. doi: 10.1073/pnas.1016024108. <a href="http://dx.doi.org/10.1073/pnas.1016024108" target="_blank">Link to article on publisher's site</a></p>
dc.identifier.issn1091-6490
dc.identifier.doi10.1073/pnas.1016024108
dc.identifier.pmid21464309
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33308
dc.description.abstractThe genes of all organisms have been shaped by selective pressures. The relationship between gene sequence and fitness has tremendous implications for understanding both evolutionary processes and functional constraints on the encoded proteins. Here, we have exploited deep sequencing technology to experimentally determine the fitness of all possible individual point mutants under controlled conditions for a nine-amino acid region of Hsp90. Over the past five decades, limited glimpses into the relationship between gene sequence and function have sparked a long debate regarding the distribution, relative proportion, and evolutionary significance of deleterious, neutral, and advantageous mutations. Our systematic experimental measurement of fitness effects of Hsp90 mutants in yeast, evaluated in the light of existing population genetic theory, are remarkably consistent with a nearly neutral model of molecular evolution.
dc.language.isoen_US
dc.publisherNational Academy of Sciences
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=21464309&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3093508/pdf/pnas.201016024.pdf
dc.subjectAmino Acid Substitution; Codon; Computer Simulation; DNA, Fungal; Evolution, Molecular; Genes, Fungal; HSP90 Heat-Shock Proteins; Models, Genetic; Models, Molecular; Phylogeny; Point Mutation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Selection, Genetic
dc.subjectEvolution
dc.subjectMolecular Biology
dc.subjectMolecular Genetics
dc.titleExperimental illumination of a fitness landscape
dc.typeJournal Article
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume108
dc.source.issue19
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1837
dc.identifier.contextkey4618830
html.description.abstract<p>The genes of all organisms have been shaped by selective pressures. The relationship between gene sequence and fitness has tremendous implications for understanding both evolutionary processes and functional constraints on the encoded proteins. Here, we have exploited deep sequencing technology to experimentally determine the fitness of all possible individual point mutants under controlled conditions for a nine-amino acid region of Hsp90. Over the past five decades, limited glimpses into the relationship between gene sequence and function have sparked a long debate regarding the distribution, relative proportion, and evolutionary significance of deleterious, neutral, and advantageous mutations. Our systematic experimental measurement of fitness effects of Hsp90 mutants in yeast, evaluated in the light of existing population genetic theory, are remarkably consistent with a nearly neutral model of molecular evolution.</p>
dc.identifier.submissionpathgsbs_sp/1837
dc.contributor.departmentProgram in Bioinformatics and Integrative Biology
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages7896-901
dc.contributor.studentRyan T. Hietpas


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