http://www.cnr.it/ontology/cnr/individuo/prodotto/ID298848
Structure and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo (Articolo in rivista)
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- Label
- Structure and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.str.2014.01.014 (literal)
- Alternative label
Romano, Maria; van de Weerd, Robert; Brouwer, Femke C. C.; Roviello, Giovanni N.; Lacroix, Ruben; Sparrius, Marion; van den Brink-van Stempvoort, Gunny; Appelmelk, Ben J.; Geurtsen, Jeroen J.; Berisio, Rita (2014)
Structure and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo
in Structure (Lond.)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Romano, Maria; van de Weerd, Robert; Brouwer, Femke C. C.; Roviello, Giovanni N.; Lacroix, Ruben; Sparrius, Marion; van den Brink-van Stempvoort, Gunny; Appelmelk, Ben J.; Geurtsen, Jeroen J.; Berisio, Rita (literal)
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- ISI Web of Science (WOS) (literal)
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- Consiglio Nazionale delle Ricerche (CNR); VU University Amsterdam (literal)
- Titolo
- Structure and Function of RNase AS, a Polyadenylate-Specific Exoribonuclease Affecting Mycobacterial Virulence In Vivo (literal)
- Abstract
- The cell-envelope of Mycobacterium tuberculosis plays a key role in bacterial virulence and antibiotic resistance. Little is known about the molecular mechanisms of regulation of cell-envelope formation. Here, we elucidate functional and structural properties of RNase AS, which modulates M. tuberculosis cell-envelope properties and strongly impacts bacterial virulence in vivo. The structure of RNase AS reveals a resemblance to RNase T from Escherichia coli, an RNase of the DEDD family involved in RNA maturation. We show that RNase AS acts as a 3 '-5 '-exoribonuclease that specifically hydrolyzes adenylate-containing RNA sequences. Also, crystal structures of complexes with AMP and UMP reveal the structural basis for the observed enzyme specificity. Notably, RNase AS shows a mechanism of substrate recruitment, based on the recognition of the hydrogen bond donor NH2 group of adenine. Our work opens a field for the design of drugs able to reduce bacterial virulence in vivo. (literal)
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