The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Yeast Carbon Catabolite Repression
Open accessAbstract
SUMMARY: Glucose and related sugars repress the transcription of genes encoding enzymes required for the utilization of alternative carbon sources; some of these genes are also repressed by other sugars such as galactose, and the process is known as catabolite repression. The different sugars produce signals which modify the conformation of certain proteins that, in turn, directly or through a regulatory cascade affect the expression of the genes subject to catabolite repression. These genes are not all controlled by a single set of regulatory proteins, but there are different circuits of repression for different groups of genes. However, the protein kinase Snf1/Cat1 is shared by the various circuits and is therefore a central element in the regulatory process. Snf1 is not operative in the presence of glucose, and preliminary evidence suggests that Snf1 is in a dephosphorylated state under these conditions. However, the enzymes that phosphorylate and dephosphorylate Snf1 have not been identified, and it is not known how the presence of glucose may affect their activity. What has been established is that Snf1 remains active in mutants lacking either the proteins Grr1/Cat80 or Hxk2 or the Glc7 complex, which functions as a protein phosphatase. One of the main roles of Snf1 is to relieve repression by the Mig1 complex, but it is also required for the operation of transcription factors such as Adr1 and possibly other factors that are still unidentified. Although our knowledge of catabolite repression is still very incomplete, it is possible in certain cases to propose a partial model of the way in which the different elements involved in catabolite repression may be integrated.
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Cites
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
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“Although Snf1, in contrast to AMPK, is not allosterically activated by AMP, it has been proposed that adenine nucleotides could also control Snf1 activity in vivo (377).”
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Wang, H., Chen, J., Hollister, K., Sowers, L. C., & Forman, B. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80348-2 · Cited by 1,636
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Gore, J., Youk, H., & van Oudenaarden, A. (2009) · Nature · doi:10.1038/nature07921 · Cited by 668
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Metadata
- Authors
- Gancedo, J. M.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 1998-06
- Volume
- 62
- Issue
- 2
- Pages
- 334-361
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- OpenAlex
- W2169875902
- Cited by
- 1,273
- References
- 3
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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