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Negative allosteric regulation of Enterococcus faecalis small alarmone synthetase RelQ by single-stranded RNA
Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet).
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2017 (engelsk)Inngår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 114, nr 14, s. 3726-3731Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The alarmone nucleotides guanosine pentaphosphate (pppGpp) and tetraphosphate (ppGpp), collectively referred to as (p)ppGpp, are key regulators of bacterial growth, stress adaptation, pathogenicity, and antibiotic tolerance. We show that the tetrameric small alarmone synthetase (SAS) RelQ from the Gram-positive pathogen Enterococcus faecalis is a sequence-specific RNA-binding protein. RelQ's enzymatic and RNA binding activities are subject to intricate allosteric regulation. (p)ppGpp synthesis is potently inhibited by the binding of single-stranded RNA. Conversely, RelQ's enzymatic activity destabilizes the RelQ: RNA complex. pppGpp, an allosteric activator of the enzyme, counteracts the effect of RNA. Tetramerization of RelQ is essential for this regulatory mechanism, because both RNA binding and enzymatic activity are abolished by deletion of the SAS-specific C-terminal helix 5 alpha. The interplay of pppGpp binding, (p)ppGpp synthesis, and RNA binding unites two archetypal regulatory paradigms within a single protein. The mechanism is likely a prevalent but previously unappreciated regulatory switch used by the widely distributed bacterial SAS enzymes.

sted, utgiver, år, opplag, sider
2017. Vol. 114, nr 14, s. 3726-3731
Emneord [en]
stringent response, (p)ppGpp, RNA-protein interaction, allosteric regulation, nucleotide signaling
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Identifikatorer
URN: urn:nbn:se:umu:diva-133722DOI: 10.1073/pnas.1617868114ISI: 000398159000059OAI: oai:DiVA.org:umu-133722DiVA, id: diva2:1093406
Tilgjengelig fra: 2017-05-05 Laget: 2017-05-05 Sist oppdatert: 2019-03-01bibliografisk kontrollert

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Andresen, LiisShingler, VickyHauryliuk, Vasili

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