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Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression.

Identifieur interne : 001874 ( Main/Exploration ); précédent : 001873; suivant : 001875

Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression.

Auteurs : Rosa M. Marion [États-Unis] ; Aviv Regev ; Eran Segal ; Yoseph Barash ; Daphne Koller ; Nir Friedman ; Erin K. O'Shea

Source :

RBID : pubmed:15353587

Descripteurs français

English descriptors

Abstract

Yeast cells modulate their protein synthesis capacity in response to physiological needs through the transcriptional control of ribosomal protein (RP) genes. Here we demonstrate that the transcription factor Sfp1, previously shown to play a role in the control of cell size, regulates RP gene expression in response to nutrients and stress. Under optimal growth conditions, Sfp1 is localized to the nucleus, bound to the promoters of RP genes, and helps promote RP gene expression. In response to inhibition of target of rapamycin (TOR) signaling, stress, or changes in nutrient availability, Sfp1 is released from RP gene promoters and leaves the nucleus, and RP gene transcription is down-regulated. Additionally, cells lacking Sfp1 fail to appropriately modulate RP gene expression in response to environmental cues. We conclude that Sfp1 integrates information from nutrient- and stress-responsive signaling pathways to help control RP gene expression.

DOI: 10.1073/pnas.0405353101
PubMed: 15353587
PubMed Central: PMC521938


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Yeast cells modulate their protein synthesis capacity in response to physiological needs through the transcriptional control of ribosomal protein (RP) genes. Here we demonstrate that the transcription factor Sfp1, previously shown to play a role in the control of cell size, regulates RP gene expression in response to nutrients and stress. Under optimal growth conditions, Sfp1 is localized to the nucleus, bound to the promoters of RP genes, and helps promote RP gene expression. In response to inhibition of target of rapamycin (TOR) signaling, stress, or changes in nutrient availability, Sfp1 is released from RP gene promoters and leaves the nucleus, and RP gene transcription is down-regulated. Additionally, cells lacking Sfp1 fail to appropriately modulate RP gene expression in response to environmental cues. We conclude that Sfp1 integrates information from nutrient- and stress-responsive signaling pathways to help control RP gene expression.</div>
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