Chlamydomonas CHT7 Is Required for an Effective Quiescent State by Regulating Nutrient-Responsive Cell Cycle Gene Expression. Issue 4 (30th April 2020)
- Record Type:
- Journal Article
- Title:
- Chlamydomonas CHT7 Is Required for an Effective Quiescent State by Regulating Nutrient-Responsive Cell Cycle Gene Expression. Issue 4 (30th April 2020)
- Main Title:
- Chlamydomonas CHT7 Is Required for an Effective Quiescent State by Regulating Nutrient-Responsive Cell Cycle Gene Expression
- Authors:
- Takeuchi, Tomomi
Sears, Barbara B.
Lindeboom, Chase
Lin, Yang-Tsung
Fekaris, Nicholas
Zienkiewicz, Krzysztof
Zienkiewicz, Agnieszka
Poliner, Eric
Benning, Christoph - Abstract:
- Abstract : The protein-interaction domains of Chlamydomonas CHT7, and not its CXC domain, are critical for nutrient-responsive regulation of cell cycle genes and consequently the entry and exit from quiescence. Abstract: COMPROMISED HYDROLYSIS OF TRIACYLGLYCEROLS7 (CHT7) in Chlamydomonas ( Chlamydomonas reinhardtii ) was previously shown to affect the transcription of a subset of genes during nitrogen (N)-replete growth and following N refeeding. Here, we show that an extensive derepression of genes involved in DNA metabolism and cell cycle–related processes, as well as downregulation of genes encoding oxidoreductases and nutrient transporters, occurs in the cht7 mutant during N deprivation. Cellular mutant phenotypes are consistent with the observed transcriptome misregulation, as cht7 cells fail to properly arrest growth, nuclear replication, and cell division following N deprivation. Reduction in cht7 colony formation following N refeeding is explained by its compromised viability during N deprivation and by the occurrence of abortive divisions during N refeeding. Surprisingly, the largely unstructured C-terminal half of CHT7 with predicted protein binding domains, but not the canonical CXC DNA binding domain, is essential for the ability of CHT7 to form stable complexes and reverse the cellular phenotypes and transcription levels in the cht7 mutant. Hence, although lacking the presumed DNA binding domain, CHT7 modulates the expression of cell cycle genes in response to NAbstract : The protein-interaction domains of Chlamydomonas CHT7, and not its CXC domain, are critical for nutrient-responsive regulation of cell cycle genes and consequently the entry and exit from quiescence. Abstract: COMPROMISED HYDROLYSIS OF TRIACYLGLYCEROLS7 (CHT7) in Chlamydomonas ( Chlamydomonas reinhardtii ) was previously shown to affect the transcription of a subset of genes during nitrogen (N)-replete growth and following N refeeding. Here, we show that an extensive derepression of genes involved in DNA metabolism and cell cycle–related processes, as well as downregulation of genes encoding oxidoreductases and nutrient transporters, occurs in the cht7 mutant during N deprivation. Cellular mutant phenotypes are consistent with the observed transcriptome misregulation, as cht7 cells fail to properly arrest growth, nuclear replication, and cell division following N deprivation. Reduction in cht7 colony formation following N refeeding is explained by its compromised viability during N deprivation and by the occurrence of abortive divisions during N refeeding. Surprisingly, the largely unstructured C-terminal half of CHT7 with predicted protein binding domains, but not the canonical CXC DNA binding domain, is essential for the ability of CHT7 to form stable complexes and reverse the cellular phenotypes and transcription levels in the cht7 mutant. Hence, although lacking the presumed DNA binding domain, CHT7 modulates the expression of cell cycle genes in response to N availability, which is essential for establishing an effective quiescent state and the coordinated resumption of growth following N refeeding. … (more)
- Is Part Of:
- The Plant Cell. Volume 32:Issue 4(2020)
- Journal:
- The Plant Cell
- Issue:
- Volume 32:Issue 4(2020)
- Issue Display:
- Volume 32, Issue 4 (2020)
- Year:
- 2020
- Volume:
- 32
- Issue:
- 4
- Issue Sort Value:
- 2020-0032-0004-0000
- Page Start:
- 1240
- Page End:
- 1269
- Publication Date:
- 2020-04-30
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.19.00628 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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- 16501.xml