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.

doi:10.1111/mmi.13874

Title: An acetylatable lysine controls CRP function in E. coli

Journal Article · Thu Nov 23 00:00:00 EST 2017 · Molecular Microbiology

DOI:https://doi.org/10.1111/mmi.13874· OSTI ID:1410133

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^[2]; Filippova, Ekaterina V. ^[3]; Kuffel, Gina ^[4]; Anderson, Wayne F. ^[3]; Gibson, Bradford W. ^[5];

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Department of Microbiology and Immunology, Stritch School of Medicine, Health Sciences Division Loyola University Chicago Maywood IL 60153 USA
Department of Biochemistry and Molecular Biology (B) and Immunology, Faculty of Chemistry University of Murcia, Campus of Espinardo, Regional Campus of International Excellence ‘‘Campus Mare Nostrum’’ Murcia E‐30100 Spain
Department of Biochemistry and Molecular Genetics Center for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine Chicago IL 60611 USA
Loyola Genomics Facility, Stritch School of Medicine, Health Sciences Division Loyola University Chicago Maywood IL 60153 USA
Buck Institute for Research on Aging Novato CA 94945 USA

Summary 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.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: DE‐SC00124430

OSTI ID:: 1410133

Journal Information:: Molecular Microbiology, Journal Name: Molecular Microbiology Vol. 107 Journal Issue: 1; ISSN 0950-382X

Publisher:: Wiley-BlackwellCopyright Statement

Country of Publication:: FAO

Language:: English

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Cited by: 22 works

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