Jeffrey M. Stein , Johanna D. Stoeckler , Li Shih-Ying , Richard L. Tolman , Malcolm MacCoss , Chen Anna , John D. Karkas , Wallace T. Ashton , Robert...
Department of Microbiology and Immunology, State UniVersity of New York Downstate Medical Center, 450 Clarkson AVenue,. Brooklyn, New York 11203, and ...
Feb 13, 2007 - Petrushanko , Aksel Soosaar , Gemma C. Atkinson , Tanel Tenson , Alexander A. Makarov , Vasili Hauryliuk. Scientific Reports 2012 2 (1), ...
subunit in initiation complexes and its joining with the 60S subunit. ... not required for its function in subunit joining but is necessary for the subsequent release of ...
ABSTRACT: The bacterial signal recognition particle (SRP) is an RNA-protein complex. In Escherichia coli, the particle consists of a 114 nt RNA, a 4.5S RNA, ...
Evidence for a Second Nucleotide Binding Site in Rat Elongation Factor eEF-2 Specific for Adenylic Nucleotides. Philippe Gonzalo, Bruno Sontag, Jean-Pierre ...
Oct 14, 1998 - The bacterial signal recognition particle (SRP) is an RNAâprotein complex. In Escherichia coli, the particle consists of a 114 nt RNA, a 4.5S ...
Interactions of Guanine Derivatives with Ethylenediamine and Diethylenetriamine. Complexes of Palladium(I1) in Solution: Pd Binding Sites of the Guanine Ring ...
Dec 29, 2009 - Jiande Gu,*,â Yaoming Xie,â¡ and Henry F. Schaefer, III*,â¡. Drug Design & DiscoVery Center, State Key Laboratory of Drug Research, Shanghai ...
Dec 29, 2009 - Electron Interaction with Phosphate Cytidine Oligomer dCpdC: Base-Centered Radical Anions and Their Electronic Spectra. Jiande Gu , Jing ...
GUANINE
NUCLEOTIDES A N D EF-G
Interactions of Periodate-Oxidized Guanine Nucleotides with Escherichia coli Elongation Factor G and the Ribosome+ James W. Bodley and Julian Gordon*
ABSTRACT:
Both periodate-oxidized G D P (GDPoX) and its KBH4-reduction product (GDPoX-red)bind to the ribosome and EF-G in the presence of fusidic acid. The complexes formed with these two nucleotides are only slightly less stable than that with G D P itself. However, the binding of both GDPoX and G D P x - r e d as observed by Millipore filtration is more dependent on the presence of fusidic acid than is the binding of GDP. A similar pattern of binding was observed with the analogous nucleotides derived from G T P (GTPOXand GTPOX-'ed) except that the y-phosphate was released on binding. However, in the usual catalytic hydrolysis reaction performed in the absence of fusidic acid, both GTPoXand GTPoX-redwere poor substrates with rates of hydrolysis