Abstract
Transcriptional regulation is the key to ensuring that proteins are expressed at the proper time and the proper amount. In Escherichia coli, the transcription factor cAMP receptor protein (CRP) is responsible for much of this regulation. Questions remain, however, regarding the regulation of CRP activity itself. Here, we demonstrate that a lysine (K100) on the surface of CRP has a dual function: to promote CRP activity at Class II promoters, and to ensure proper CRP steady state levels. Both functions require the lysine's positive charge; intriguingly, the positive charge of K100 can be neutralized by acetylation using the central metabolite acetyl phosphate as the acetyl donor. We propose that CRP K100 acetylation could be a mechanism by which the cell downwardly tunes CRP-dependent Class II promoter activity, whilst elevating CRP steady state levels, thus indirectly increasing Class I promoter activity. This mechanism would operate under conditions that favor acetate fermentation, such as during growth on glucose as the sole carbon source or when carbon flux exceeds the capacity of the central metabolic pathways.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 116-131 |
| Number of pages | 16 |
| Journal | Molecular Microbiology |
| Volume | 107 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 2018 |
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ASJC Scopus subject areas
- Microbiology
- Molecular Biology
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An acetylatable lysine controls CRP function in E. coli. / Davis, Robert; Écija-Conesa, Ana; Gallego-Jara, Julia; de Diego, Teresa; Filippova, Ekaterina V.; Kuffel, Gina; Anderson, Wayne F; Gibson, Bradford W.; Schilling, Birgit; Canovas, Manuel; Wolfe, Alan J.
In: Molecular Microbiology, Vol. 107, No. 1, 01.01.2018, p. 116-131.Research output: Contribution to journal › Article
TY - JOUR
T1 - An acetylatable lysine controls CRP function in E. coli
AU - Davis, Robert
AU - Écija-Conesa, Ana
AU - Gallego-Jara, Julia
AU - de Diego, Teresa
AU - Filippova, Ekaterina V.
AU - Kuffel, Gina
AU - Anderson, Wayne F
AU - Gibson, Bradford W.
AU - Schilling, Birgit
AU - Canovas, Manuel
AU - Wolfe, Alan J.
PY - 2018/1/1
Y1 - 2018/1/1
N2 - Transcriptional regulation is the key to ensuring that proteins are expressed at the proper time and the proper amount. In Escherichia coli, the transcription factor cAMP receptor protein (CRP) is responsible for much of this regulation. Questions remain, however, regarding the regulation of CRP activity itself. Here, we demonstrate that a lysine (K100) on the surface of CRP has a dual function: to promote CRP activity at Class II promoters, and to ensure proper CRP steady state levels. Both functions require the lysine's positive charge; intriguingly, the positive charge of K100 can be neutralized by acetylation using the central metabolite acetyl phosphate as the acetyl donor. We propose that CRP K100 acetylation could be a mechanism by which the cell downwardly tunes CRP-dependent Class II promoter activity, whilst elevating CRP steady state levels, thus indirectly increasing Class I promoter activity. This mechanism would operate under conditions that favor acetate fermentation, such as during growth on glucose as the sole carbon source or when carbon flux exceeds the capacity of the central metabolic pathways.
AB - Transcriptional regulation is the key to ensuring that proteins are expressed at the proper time and the proper amount. In Escherichia coli, the transcription factor cAMP receptor protein (CRP) is responsible for much of this regulation. Questions remain, however, regarding the regulation of CRP activity itself. Here, we demonstrate that a lysine (K100) on the surface of CRP has a dual function: to promote CRP activity at Class II promoters, and to ensure proper CRP steady state levels. Both functions require the lysine's positive charge; intriguingly, the positive charge of K100 can be neutralized by acetylation using the central metabolite acetyl phosphate as the acetyl donor. We propose that CRP K100 acetylation could be a mechanism by which the cell downwardly tunes CRP-dependent Class II promoter activity, whilst elevating CRP steady state levels, thus indirectly increasing Class I promoter activity. This mechanism would operate under conditions that favor acetate fermentation, such as during growth on glucose as the sole carbon source or when carbon flux exceeds the capacity of the central metabolic pathways.
UR - http://www.scopus.com/inward/record.url?scp=85034760683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85034760683&partnerID=8YFLogxK
U2 - 10.1111/mmi.13874
DO - 10.1111/mmi.13874
M3 - Article
C2 - 29105190
AN - SCOPUS:85034760683
VL - 107
SP - 116
EP - 131
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 1
ER -