Domain organization of the yeast histone chaperone FACT: The conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress

Allyson F. O'Donnell; Neil K. Brewster; Joelius Kurniawan; Laura V. Minard; Gerald C. Johnston; Richard A. Singer

doi:10.1093/nar/gkh922

Domain organization of the yeast histone chaperone FACT: The conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress

Allyson F. O'Donnell, Neil K. Brewster, Joelius Kurniawan, Laura V. Minard, Gerald C. Johnston, Richard A. Singer

Medicine

Résultat de recherche: Article › examen par les pairs

40 Citations (Scopus)

Résumé

The abundant nuclear complex termed FACT affects several DNA transactions in a chromatin context, including transcription, replication, and repair. Earlier studies of yeast FACT, which indicated the apparent dispensability of conserved sequences at the N terminus of the FACT subunit Cdc68/Spt16, prompted genetic and biochemical studies reported here that suggest the domain organization for Spt16 and the other FACT subunit Pob3, the yeast homolog of the metazoan SSRP1 protein. Our findings suggest that each FACT subunit is a multidomain protein, and that FACT integrity depends on Pob3 interactions with the Spt16 Mid domain. The conserved Spt16 N-terminal domain (NTD) is shown to be without essential function during normal growth, but becomes important under conditions of replication stress. Genetic interactions suggest that some functions carried out by the Spt16 NTD may be partially redundant within FACT.

Langue d'origine	English
Pages (de-à)	5894-5906
Nombre de pages	13
Journal	Nucleic Acids Research
Volume	32
Numéro de publication	19
DOI	https://doi.org/10.1093/nar/gkh922
Statut de publication	Published - 2004

Note bibliographique

Funding Information:
We thank Steve Elledge, Tim Formosa, LeAnn Howe and Jerry Workman for plasmids, Jeff Coles for preliminary experiments, David Carruthers and Kendra Gillis for technical assistance, and Chris Barnes for helpful discussions. This work was supported by a grant from the Canadian Institutes of Health Research. A.F.O. was supported by the Natural Sciences and Engineering Research Council of Canada, the Canadian Institutes of Health Research, the Killam Foundation and the Nova Scotia Health Research Foundation. J.K. was supported by the Canadian Institutes of Health Research; L.V.M. was supported by grants from the Dalhousie Cancer Biology Research Group.

ASJC Scopus Subject Areas

Genetics

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't

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10.1093/nar/gkh922

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title = "Domain organization of the yeast histone chaperone FACT: The conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress",

abstract = "The abundant nuclear complex termed FACT affects several DNA transactions in a chromatin context, including transcription, replication, and repair. Earlier studies of yeast FACT, which indicated the apparent dispensability of conserved sequences at the N terminus of the FACT subunit Cdc68/Spt16, prompted genetic and biochemical studies reported here that suggest the domain organization for Spt16 and the other FACT subunit Pob3, the yeast homolog of the metazoan SSRP1 protein. Our findings suggest that each FACT subunit is a multidomain protein, and that FACT integrity depends on Pob3 interactions with the Spt16 Mid domain. The conserved Spt16 N-terminal domain (NTD) is shown to be without essential function during normal growth, but becomes important under conditions of replication stress. Genetic interactions suggest that some functions carried out by the Spt16 NTD may be partially redundant within FACT.",

author = "O'Donnell, {Allyson F.} and Brewster, {Neil K.} and Joelius Kurniawan and Minard, {Laura V.} and Johnston, {Gerald C.} and Singer, {Richard A.}",

note = "Funding Information: We thank Steve Elledge, Tim Formosa, LeAnn Howe and Jerry Workman for plasmids, Jeff Coles for preliminary experiments, David Carruthers and Kendra Gillis for technical assistance, and Chris Barnes for helpful discussions. This work was supported by a grant from the Canadian Institutes of Health Research. A.F.O. was supported by the Natural Sciences and Engineering Research Council of Canada, the Canadian Institutes of Health Research, the Killam Foundation and the Nova Scotia Health Research Foundation. J.K. was supported by the Canadian Institutes of Health Research; L.V.M. was supported by grants from the Dalhousie Cancer Biology Research Group.",

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AU - Johnston, Gerald C.

AU - Singer, Richard A.

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Domain organization of the yeast histone chaperone FACT: The conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress

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PubMed: MeSH publication types

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