Post-translational Modification by β-Lysylation Is Required for Activity of Escherichia coli Elongation Factor P (EF-P)
Authors:
- Hans E. JohanssonHJHans E. Johansson
- Hiroyuki AokiHAHiroyuki Aoki
- Bill X. HuangBHBill X. Huang
- Hee-Yong KimHKHee-Yong Kim
- M. Clelia GanozaMGM. Clelia Ganoza
- Myung Hee ParkMPMyung Hee Park
Open Access
- 1 January 2012
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 287 (4) , 2579-2590
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysineNature Chemical Biology, 2011
- Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiaeProceedings of the National Academy of Sciences, 2011
- Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymesProtein Engineering, Design and Selection, 2010
- PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella entericaMolecular Cell, 2010
- A bacterial ortholog of class II lysyl‐tRNA synthetase activates lysineFEBS Letters, 2010
- Functional significance of eIF5A and its hypusine modification in eukaryotesAmino Acids, 2009
- Hypusine-containing protein eIF5A promotes translation elongationNature, 2009
- Following movement of the L1 stalk between three functional states in single ribosomesProceedings of the National Academy of Sciences, 2009
- Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidineProceedings of the National Academy of Sciences, 2008
- Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-AminomutasesBiochemistry, 2006