Show simple item record

dc.contributor.authorMorey, Lisa
dc.contributor.authorBarnes, Kelly
dc.contributor.authorChen, Yinhuai
dc.contributor.authorFitzgerald-Hayes, Molly
dc.contributor.authorBaker, Richard E.
dc.date2022-08-11T08:10:02.000
dc.date.accessioned2022-08-23T16:53:02Z
dc.date.available2022-08-23T16:53:02Z
dc.date.issued2004-12-14
dc.date.submitted2008-07-09
dc.identifier.citationEukaryot Cell. 2004 Dec;3(6):1533-43. <a href="http://dx.doi.org/10.1128/EC.3.6.1533-1543.2004">Link to article on publisher's site</a>
dc.identifier.issn1535-9778 (Print)
dc.identifier.doi10.1128/EC.3.6.1533-1543.2004
dc.identifier.pmid15590827
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42181
dc.description.abstractCentromere-specific H3-like proteins (CenH3s) are conserved across the eukaryotic kingdom and are required for packaging centromere DNA into a specialized chromatin structure required for kinetochore assembly. Cse4 is the CenH3 protein of the budding yeast Saccharomyces cerevisiae. Like all CenH3 proteins, Cse4 consists of a conserved histone fold domain (HFD) and a divergent N terminus (NT). The Cse4 NT contains an essential domain designated END (for essential N-terminal domain); deletion of END is lethal. To investigate the role of the Cse4 NT in centromere targeting, a series of deletion alleles (cse4DeltaNT) were analyzed. No part of the Cse4 NT was required to target mutant proteins to centromere DNA in the presence of functional Cse4. A Cse4 degron strain was used to examine targeting of a Cse4DeltaNT protein in the absence of wild-type Cse4. The END was not required for centromere targeting under these conditions, confirming that the HFD confers specificity of Cse4 centromere targeting. Surprisingly, overexpression of the HFD bypassed the requirement for the END altogether, and viable S. cerevisiae strains in which the cells express only the Cse4 HFD and six adjacent N-terminal amino acids (Cse4Delta129) were constructed. Despite the complete absence of the NT, mitotic chromosome loss in the cse4Delta129 strain increased only 6-fold compared to a 15-fold increase in strains overexpressing wild-type Cse4. Thus, when overexpressed, the Cse4 HFD is sufficient for centromere function in S. cerevisiae, and no posttranslational modification or interaction of the NT with other kinetochore component(s) is essential for accurate chromosome segregation in budding yeast.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=15590827&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAlleles
dc.subjectBlotting, Northern
dc.subjectBlotting, Southern
dc.subjectCentromere
dc.subjectChromatin
dc.subjectChromatin Immunoprecipitation
dc.subjectChromosomal Proteins, Non-Histone
dc.subjectFungal Proteins
dc.subjectGene Deletion
dc.subjectGenetic Complementation Test
dc.subjectGenotype
dc.subjectGlucose
dc.subjectHistones
dc.subjectKinetochores
dc.subjectModels, Biological
dc.subjectModels, Genetic
dc.subjectMutation
dc.subjectPhenotype
dc.subjectPlasmids
dc.subjectProtein Folding
dc.subjectProtein Processing, Post-Translational
dc.subjectProtein Structure, Tertiary
dc.subjectSaccharomyces cerevisiae
dc.subjectTime Factors
dc.subjectMicrobiology
dc.subjectMolecular Genetics
dc.titleThe histone fold domain of Cse4 is sufficient for CEN targeting and propagation of active centromeres in budding yeast
dc.typeJournal Article
dc.source.journaltitleEukaryotic cell
dc.source.volume3
dc.source.issue6
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1550&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/551
dc.identifier.contextkey545033
refterms.dateFOA2022-08-23T16:53:02Z
html.description.abstract<p>Centromere-specific H3-like proteins (CenH3s) are conserved across the eukaryotic kingdom and are required for packaging centromere DNA into a specialized chromatin structure required for kinetochore assembly. Cse4 is the CenH3 protein of the budding yeast Saccharomyces cerevisiae. Like all CenH3 proteins, Cse4 consists of a conserved histone fold domain (HFD) and a divergent N terminus (NT). The Cse4 NT contains an essential domain designated END (for essential N-terminal domain); deletion of END is lethal. To investigate the role of the Cse4 NT in centromere targeting, a series of deletion alleles (cse4DeltaNT) were analyzed. No part of the Cse4 NT was required to target mutant proteins to centromere DNA in the presence of functional Cse4. A Cse4 degron strain was used to examine targeting of a Cse4DeltaNT protein in the absence of wild-type Cse4. The END was not required for centromere targeting under these conditions, confirming that the HFD confers specificity of Cse4 centromere targeting. Surprisingly, overexpression of the HFD bypassed the requirement for the END altogether, and viable S. cerevisiae strains in which the cells express only the Cse4 HFD and six adjacent N-terminal amino acids (Cse4Delta129) were constructed. Despite the complete absence of the NT, mitotic chromosome loss in the cse4Delta129 strain increased only 6-fold compared to a 15-fold increase in strains overexpressing wild-type Cse4. Thus, when overexpressed, the Cse4 HFD is sufficient for centromere function in S. cerevisiae, and no posttranslational modification or interaction of the NT with other kinetochore component(s) is essential for accurate chromosome segregation in budding yeast.</p>
dc.identifier.submissionpathoapubs/551
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages1533-43


Files in this item

Thumbnail
Name:
15590827.pdf
Size:
374.1Kb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record