Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Interaction of the sarcin/ricin domain of 23 S ribosomal RNA with proteinsL3 and L6
Autore:
Uchiumi, T; Sato, N; Wada, A; Hachimori, A;
Indirizzi:
Shinshu868567,Fac Text Sci & Technol, Inst High Polymer Res, Ueda, Nagano 3 Shinshu Univ Ueda Nagano Japan 3868567 t High Polymer Res, Ueda, Nagano 3 Osaka Med Coll, Dept Phys, Takatsuki, Osaka 5690084, Japan Osaka Med CollTakatsuki Osaka Japan 5690084 atsuki, Osaka 5690084, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 274, anno: 1999,
pagine: 681 - 686
SICI:
0021-9258(19990108)274:2<681:IOTSDO>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI RIBOSOME; ELONGATION FACTOR-G; RICIN-A-CHAIN; ANTIBIOTIC THIOSTREPTON; BINDING-SITES; CROSS-LINKING; GTPASE CENTER; ALPHA-SARCIN; 50S SUBUNIT; FACTOR TU;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Uchiumi, T Shinshu868567,Fac Text Sci & Technol, Inst High Polymer Res, Ueda, Nagano 3 Shinshu Univ Ueda Nagano Japan 3868567 mer Res, Ueda, Nagano 3
Citazione:
T. Uchiumi et al., "Interaction of the sarcin/ricin domain of 23 S ribosomal RNA with proteinsL3 and L6", J BIOL CHEM, 274(2), 1999, pp. 681-686

Abstract

We investigated interaction of an RNA domain covering the target;site of alpha-sarcin and ricin (sarcin/ricin domain) of Escherichia coil 23 S rRNA with ribosomal proteins. RNA fragments comprising residues 2630-2788 (Tox-1)and residues 2840-2774 (Tox-2) of 23 S rRNA were transcribed in vitro and used to analyze the binding proteins by gel shift and filter binding. Protein L6 ;bound to both Tox-1 (K-d: 0.31 mu M) and Tox-2 (K-d: 0.18 mu M), andL3 bound only to Tox-1 (K-d: 0.069 mu M) in a solution containing 10 mM MgCl2 and 175 mM KCl at 0 degrees C. Footprinting studies were performed using the chemical probe dimethyl sulfate on full-length 23 S rRNA, Binding of L6 protected a single base, A-2757, and strongly enhanced reactivity of C-2752, A direct role of A-2757 in the L6 binding was verified by site-directed mutagenesis; replacements of A-2757 with G and C impaired the 1.6 binding. On the other hand, binding of L3 protected A-2632, A-2634, A-2635, A-2675, A-2726, A-2733, A-2749, and A-2750. Interestingly, binding of L6 and L3 together protected additional bases A-2657, A-2662, C-2666, and C-2667 in the sarcin/ricin loop, in addition to A-2740, A-2741, A-2748, A-2753, A-2764,A-2765, and A-2766 in the other stem-loop. This appears to be due to cooperative interaction of L3 and L6 with the RNA. The results are discussed with respect to conformational modulation of the sarcin/ricin domain by the protein binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:07:45