Aug, 1998
Crm1 (Xpol) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress
GENES TO CELLS
- ,
- ,
- ,
- Volume
- 3
- Number
- 8
- First page
- 521
- Last page
- 532
- Language
- English
- Publishing type
- DOI
- 10.1046/j.1365-2443.1998.00209.x
- Publisher
- BLACKWELL SCIENCE LTD
Background: The yAP-1 transcription factor is crucial for the oxidative stress response of the budding yeast Saccharomyces cerevisiae; its activity is induced in response to oxidative stress, and as a consequence the expression of a number of target genes is enhanced. We have shown previously that yAP-1 is mainly found in the cytoplasm, but that upon the imposition of oxidative stress it localizes to the nucleus. In this study, we addressed the mechanism through which yAP-1 nuclear localization is regulated.
Results: Here we show that yAP-1 localization is mediated by active export from the nucleus, resulting from the activity of Crm1 (XpoI), a conserved protein that functions as an export receptor which recognizes the nuclear export signal (NES). When Crm1 expression was repressed, yAP-1 was localized in the nucleus and induced the expression of a yAP-1 dependent target gene. Our results also suggest that the cysteine rich domain (CRD), at the C-terminus of yAP-1, functions as an export recognition sequence, yAP-1 and Crm1 interact in vivo and this interaction is reduced in response to oxidative stress.
Conclusions: These results suggest a novel regulatory mechanism of nucleocytoplasmic transport which is dependent upon a redox sensitive nuclear export pathway.
Results: Here we show that yAP-1 localization is mediated by active export from the nucleus, resulting from the activity of Crm1 (XpoI), a conserved protein that functions as an export receptor which recognizes the nuclear export signal (NES). When Crm1 expression was repressed, yAP-1 was localized in the nucleus and induced the expression of a yAP-1 dependent target gene. Our results also suggest that the cysteine rich domain (CRD), at the C-terminus of yAP-1, functions as an export recognition sequence, yAP-1 and Crm1 interact in vivo and this interaction is reduced in response to oxidative stress.
Conclusions: These results suggest a novel regulatory mechanism of nucleocytoplasmic transport which is dependent upon a redox sensitive nuclear export pathway.
- Link information
-
- DOI
- https://doi.org/10.1046/j.1365-2443.1998.00209.x
- CiNii Articles
- http://ci.nii.ac.jp/naid/80010611558
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/9797454
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000076791200004&DestApp=WOS_CPL
- ID information
-
- DOI : 10.1046/j.1365-2443.1998.00209.x
- ISSN : 1356-9597
- CiNii Articles ID : 80010611558
- Pubmed ID : 9797454
- Web of Science ID : WOS:000076791200004