Interaction of Mycobacterium tuberculosis Elongation Factor Tu with 1 GTP is regulated by phosphorylation
نویسندگان
چکیده
3 Andaleeb Sajid, Gunjan Arora, Meetu Gupta, Anshika Singhal, Kausik Chakraborty, Vinay 4 Kumar Nandicoori and Yogendra Singh 5 6 Institute of Genomics and Integrative Biology (CSIR), Delhi-110007, India 7 National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi-110067, India 8 9 10 11 Running title: Regulation of mycobacterial Ef-Tu by phosphorylation 12 13 14 15 *Corresponding Address: 16 17 Yogendra Singh, Ph.D. 18 Institute of Genomics and Integrative Biology (CSIR), 19 Mall Road, Delhi -110007, India. 20 Tel: +11 2766 6156; Fax: +11 2766 7471, 21 E-mail: [email protected] 22 Copyright © 2011, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.05469-11 JB Accepts, published online ahead of print on 29 July 2011
منابع مشابه
Interaction of Mycobacterium tuberculosis elongation factor Tu with GTP is regulated by phosphorylation.
During protein synthesis, translation elongation factor Tu (Ef-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the acceptor site on the ribosome. The activity of Ef-Tu is dependent on its interaction with GTP. Posttranslational modifications, such as phosphorylation, are known to regulate the activity of Ef-Tu in several prokaryotes. Although a study of the Myc...
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The interaction of protein synthesis elongation factor 1 (EF-1) from wheat embryos and elongation factor Tu from Escherichia coli with cytidylyl(5’-3’)guanosine 5’-triphosphate(pppGpC) has been studied. The dinucleotide 5’-triphosphate interacts strongly with EF-1 as evidenced by its capacity to inhibit the binding of [3H]GTP to the factor. The analogs pGpC and GpC do not interfere with GTP bin...
متن کاملThe crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
BACKGROUND Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS The crystal structure of EF-Tu from Thermus aquaticus, complexe...
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Aurodox is a member of the family of kirromycin antibiotics, which inhibit protein biosynthesis by binding to elongation factor Tu (EF-Tu). We have determined the crystal structure of the 1:1:1 complex of Thermus thermophilus EF-Tu with GDP and aurodox to 2.0-Å resolution. During its catalytic cycle, EF-Tu adopts two strikingly different conformations depending on the nucleotide bound: the GDP ...
متن کاملConformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox.
Aurodox is a member of the family of kirromycin antibiotics, which inhibit protein biosynthesis by binding to elongation factor Tu (EF-Tu). We have determined the crystal structure of the 1:1:1 complex of Thermus thermophilus EF-Tu with GDP and aurodox to 2.0-A resolution. During its catalytic cycle, EF-Tu adopts two strikingly different conformations depending on the nucleotide bound: the GDP ...
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