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Titolo:
Reversible inhibition of protein splicing by zinc ion
Autore:
Mills, KV; Paulus, H;
Indirizzi:
Boston Biomed Res Inst, Watertown, MA 02742 USA Boston Biomed Res Inst Watertown MA USA 02742 st, Watertown, MA 02742 USA Harvard Univ, Dept Chem & Chem Biol, Cambridge, MA 02138 USA Harvard UnivCambridge MA USA 02138 & Chem Biol, Cambridge, MA 02138 USA Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 em & Mol Pharmacol, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 14, volume: 276, anno: 2001,
pagine: 10832 - 10838
SICI:
0021-9258(20010406)276:14<10832:RIOPSB>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUBERCULOSIS RECA INTEIN; MINIMAL INTEIN; SPLIT INTEIN; DNAE GENE; IN-VITRO; BINDING; PCC6803;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Paulus, H Boston Biomed Res Inst, 64 Grove St, Watertown, MA 02742 USA Boston Biomed Res Inst 64 Grove St Watertown MA USA 02742 42 USA
Citazione:
K.V. Mills e H. Paulus, "Reversible inhibition of protein splicing by zinc ion", J BIOL CHEM, 276(14), 2001, pp. 10832-10838

Abstract

Protein splicing involves the self-catalyzed excision of a protein-splicing element, the intein, from flanking polypeptides, the exteins, which are concomitantly joined by a peptide bond. Taking advantage of recently developed in vitro systems in which protein splicing occurs in trans to assay for protein-splicing inhibitors, we discovered that low concentrations of Zn2+ inhibited splicing mediated both by the RecA intein from Mycobacterium tuberculosis and by the naturally split DnaE intein from Synechocystis sp. PCC6803. Inhibition by Zn2+ was also observed with a cis-splicing system involving the RecA intein. In all experimental systems used, inhibition by Zn2+ could be completely reversed by the addition of EDTA. Zinc ion also inhibited hydroxylamine-dependent N-terminal cleavage of the RecA intein. All otherdivalent transition metal ions tested were less effective as inhibitors than Zn2+. The reversible inhibition by Zn2+ should be useful in studies of the mechanism of protein splicing and allow structural studies of unmodifiedprotein-splicing precursors.

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Documento generato il 19/09/20 alle ore 09:16:13