skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Authors:
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [2]; ORCiD logo [2];  [3];  [4];  [3];  [5]; ORCiD logo [5]; ORCiD logo [2]; ORCiD logo [1]
  1. Department of Microbiology and Immunology, Stritch School of Medicine, Health Sciences Division, Loyola University Chicago, Maywood IL 60153 USA
  2. 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
  3. Department of Biochemistry and Molecular Genetics, Center for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago IL 60611 USA
  4. Loyola Genomics Facility, Stritch School of Medicine, Health Sciences Division, Loyola University Chicago, Maywood IL 60153 USA
  5. Buck Institute for Research on Aging, Novato CA 94945 USA
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1410133
Grant/Contract Number:
SC00124430
Resource Type:
Journal Article: Publisher's Accepted Manuscript
Journal Name:
Molecular microbiology
Additional Journal Information:
Journal Volume: 107; Journal Issue: 1; Related Information: CHORUS Timestamp: 2017-12-23 06:21:17; Journal ID: ISSN 0950-382X
Publisher:
Wiley-Blackwell
Country of Publication:
FAO
Language:
English

Citation Formats

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, and Wolfe, Alan J.. An acetylatable lysine controls CRP function in E. coli: Acetylatable lysine controls. FAO: N. p., 2017. Web. doi:10.1111/mmi.13874.
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.. An acetylatable lysine controls CRP function in E. coli: Acetylatable lysine controls. FAO. doi:10.1111/mmi.13874.
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, and Wolfe, Alan J.. 2017. "An acetylatable lysine controls CRP function in E. coli: Acetylatable lysine controls". FAO. doi:10.1111/mmi.13874.
@article{osti_1410133,
title = {An acetylatable lysine controls CRP function in E. coli: Acetylatable lysine controls},
author = {Davis, Robert and Écija-Conesa, Ana and Gallego-Jara, Julia and de Diego, Teresa and Filippova, Ekaterina V. and Kuffel, Gina and Anderson, Wayne F. and Gibson, Bradford W. and Schilling, Birgit and Canovas, Manuel and Wolfe, Alan J.},
abstractNote = {},
doi = {10.1111/mmi.13874},
journal = {Molecular microbiology},
number = 1,
volume = 107,
place = {FAO},
year = 2017,
month =
}

Journal Article:
Free Publicly Available Full Text
This content will become publicly available on November 23, 2018
Publisher's Accepted Manuscript

Save / Share:
  • Menaquinone biosynthesis is initiated by the conversion of chorismate to isochorismate, a reaction that is catalyzed by the menaquinone-specific isochorismate synthase, MenF. The catalytic mechanism of MenF has been probed using a combination of structural and biochemical studies, including the 2.5 {angstrom} structure of the enzyme, and Lys190 has been identified as the base that activates water for nucleophilic attack at the chorismate C2 carbon. MenF is a member of a larger family of Mg{sup 2+} dependent chorismate binding enzymes catalyzing distinct chorismate transformations. The studies reported here extend the mechanism recently proposed for this enzyme family by He etmore » al.: He, Z., Stigers Lavoie, K. D., Bartlett, P. A., and Toney, M. D. (2004) J. Am. Chem. Soc. 126, 2378-85.« less
  • The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222{sub 1}; the Ta{sub 6}Br{sub 12}{sup 2+} cluster was used to derivatize the C2 crystals. The method of single isomorphous replacement with anomalous scattering (SIRAS) as implemented in SHELXD was used to solve the Ta{sub 6}Br{sub 12}{sup 2+}-derivatized structure to 5 {angstrom} resolution. Many of the Ta{sub 6}Br{sub 12}{sup 2+}-binding sites had twofold and fivefold noncrystallographic symmetry. Taking advantage of this feature, phase modification was performed in DM. The electron-density map of LdcI displays many features in agreement with the low-resolution negative-stain electron-densitymore » map [Snider et al. (2006), J. Biol. Chem. 281, 1532-1546].« less
  • A new method has been developed to couple a lysine-reactive cross-linker to the 4-thiouridine residue at position 8 in the primary structure of the Escherichia coli initiator methionine tRNA (tRNA/sup fMet/). Incubation of the affinity-labeling tRNA/sup fMet/ derivative with E. coli methionyl-tRNA synthetase (MetRS) yielded a covalent complex of the protein and nucleic acid and resulted in loss of amino acid acceptor activity of the enzyme. A stoichiometric relationship (1:1) was observed between the amount of cross-linked tRNA and the amount of enzyme inactivated. Cross-linking was effectively inhibited by unmodified tRNA/sup fMet/, but not by noncognate tRNA/sup Phe/. The covalentmore » complex was digested with trypsin, and the resulting tRNA-bound peptides were purified from excess free peptides by anion-exchange chromatography. The tRNA was then degraded with T1 ribonuclease, and the peptides bound to the 4-thiouridine-containing dinucleotide were purified by high-pressure liquid chromatography. Two major peptide products were isolated plus several minor peptides. N-Terminal sequencing of the peptides obtained in highest yield revealed that the 4-thiouridine was cross-linked to lysine residues 402 and 439 in the primary sequence of MetRS. Since many prokaryotic tRNAs contain 4-thiouridine, the procedures described here should prove useful for identification of peptide sequences near this modified base when a variety of tRNAs are bound to specific proteins.« less
  • Inactivation of Escherichia coli DNA polymerase I by pyridoxal 5'-phosphate treatment results from its reactivity at multiple lysine residues. One of these residues, lysine-758, has been shown to be located at the substrate binding site in DNA polymerase I. We now demonstrate that lysine-635 is another important target of pyridoxylation; modification of this site results in decreased rates of DNA synthesis. Addition of template-primer with or without substrate deoxynucleoside triphosphate protects lysine-635 from pyridoxylation. Analysis of the initiation versus elongation phase of DNA synthesis by lysine-635-modified enzyme revealed that elongation of the DNA chain is severely affected by the lysine-635more » modification. We therefore conclude that this lysine residue plays an important role in the processive mode of DNA synthesis by E. coli DNA polymerase I.« less