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dc.contributor.authorBaker, Richard E.
dc.contributor.authorRogers, Kelly
dc.date2022-08-11T08:10:03.000
dc.date.accessioned2022-08-23T16:53:16Z
dc.date.available2022-08-23T16:53:16Z
dc.date.issued2006-10-10
dc.date.submitted2008-07-15
dc.identifier.citation<p>Genetics. 2006 Nov;174(3):1481-92. Epub 2006 Oct 8. <a href="http://dx.doi.org/10.1534/genetics.106.062794">Link to article on publisher's site</a></p>
dc.identifier.issn0016-6731 (Print)
dc.identifier.doi10.1534/genetics.106.062794
dc.identifier.pmid17028330
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42236
dc.description.abstractCentromere H3 proteins (CenH3's) are variants of histone H3 specialized for packaging centromere DNA. Unlike canonical H3, which is among the most conserved of eukaryotic proteins, CenH3's are rapidly evolving, raising questions about orthology and conservation of function across species. To gain insight on CenH3 evolution and function, a phylogenetic analysis was undertaken on CenH3 proteins drawn from a single, ancient lineage, the Fungi. Using maximum-likelihood methods, a credible phylogeny was derived for the conserved histone fold domain (HFD) of 25 fungal CenH3's. The collection consisted mostly of hemiascomycetous yeasts, but also included basidiomycetes, euascomycetes, and an archaeascomycete. The HFD phylogeny closely recapitulated known evolutionary relationships between the species, supporting CenH3 orthology. The fungal CenH3's lacked significant homology in their N termini except for those of the Saccharomyces/Kluyveromyces clade that all contained a region homologous to the essential N-terminal domain found in Saccharomyces cerevisiae Cse4. The ability of several heterologous CenH3's to function in S. cerevisiae was tested and found to correlate with evolutionary distance. Domain swapping between S. cerevisiae Cse4 and the noncomplementing Pichia angusta ortholog showed that species specificity could not be explained by the presence or absence of any recognized secondary structural element of the HFD.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17028330&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1667059/
dc.subjectAmino Acid Sequence
dc.subjectCentromere
dc.subjectDNA, Fungal
dc.subjectEvolution, Molecular
dc.subjectFungal Proteins
dc.subjectGenes, Fungal
dc.subjectGenetic Complementation Test
dc.subjectHistones
dc.subjectLikelihood Functions
dc.subjectMolecular Sequence Data
dc.subject*Phylogeny
dc.subjectProtein Folding
dc.subjectProtein Structure, Tertiary
dc.subjectSaccharomyces cerevisiae
dc.subjectSequence Analysis, DNA
dc.subjectSequence Homology, Amino Acid
dc.subjectSpecies Specificity
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titlePhylogenetic analysis of fungal centromere H3 proteins
dc.typeJournal Article
dc.source.journaltitleGenetics
dc.source.volume174
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/601
dc.identifier.contextkey549030
html.description.abstract<p>Centromere H3 proteins (CenH3's) are variants of histone H3 specialized for packaging centromere DNA. Unlike canonical H3, which is among the most conserved of eukaryotic proteins, CenH3's are rapidly evolving, raising questions about orthology and conservation of function across species. To gain insight on CenH3 evolution and function, a phylogenetic analysis was undertaken on CenH3 proteins drawn from a single, ancient lineage, the Fungi. Using maximum-likelihood methods, a credible phylogeny was derived for the conserved histone fold domain (HFD) of 25 fungal CenH3's. The collection consisted mostly of hemiascomycetous yeasts, but also included basidiomycetes, euascomycetes, and an archaeascomycete. The HFD phylogeny closely recapitulated known evolutionary relationships between the species, supporting CenH3 orthology. The fungal CenH3's lacked significant homology in their N termini except for those of the Saccharomyces/Kluyveromyces clade that all contained a region homologous to the essential N-terminal domain found in Saccharomyces cerevisiae Cse4. The ability of several heterologous CenH3's to function in S. cerevisiae was tested and found to correlate with evolutionary distance. Domain swapping between S. cerevisiae Cse4 and the noncomplementing Pichia angusta ortholog showed that species specificity could not be explained by the presence or absence of any recognized secondary structural element of the HFD.</p>
dc.identifier.submissionpathoapubs/601
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages1481-92


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