Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Frindert, Jens [VerfasserIn]   i
 Zhang, Yaqing [VerfasserIn]   i
 Ahmed, Yasar Luqman [VerfasserIn]   i
 Sinning, Irmgard [VerfasserIn]   i
 Jäschke, Andres [VerfasserIn]   i
Titel:YvcI from Bacillus subtilis has in vitro RNA pyrophosphohydrolase activity
Verf.angabe:Jens Frindert, Masroor Ahmad Kahloon, Yaqing Zhang, Yasar Luqman Ahmed, Irmgard Sinning, and Andres Jäschke
E-Jahr:2019
Jahr:November 18, 2019
Umfang:11 S.
Fussnoten:Gesehen am 17.01.2020
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : Soc., 1905
Jahr Quelle:2019
Band/Heft Quelle:294(2019), 52, Seite 19967-19977
ISSN Quelle:1083-351X
Abstract:RNA degradation is one of several ways for organisms to regulate gene expression. In bacteria, the removal of two terminal phosphate moieties as orthophosphate (Bacillus subtilis) or pyrophosphate (Escherichia coli) triggers ribonucleolytic decay of primary transcripts by 5′-monophosphate-dependent ribonucleases. In the soil-dwelling firmicute species B. subtilis, the RNA pyrophosphohydrolase BsRppH, a member of the Nudix family, triggers RNA turnover by converting primary transcripts to 5′-monophospate RNA. In addition to BsRppH, a source of redundant activity in B. subtilis has been proposed. Here, using recombinant protein expression and in vitro enzyme assays, we provide evidence for several additional RNA pyrophosphohydrolases, among them MutT, NudF, YmaB, and YvcI in B. subtilis. We found that in vitro, YvcI converts RNA 5′-di- and triphosphates into monophosphates in the presence of manganese at neutral to slightly acidic pH. It preferred G-initiating RNAs and required at least one unpaired nucleotide at the 5′-end of its substrates, with the 5′-terminal nucleotide determining whether primarily ortho- or pyrophosphate is released. Exchanges of catalytically important glutamate residues in the Nudix motif impaired or abolished the enzymatic activity of YvcI. In summary, the results of our extensive in vitro biochemical characterization raise the possibility that YvcI is an additional RNA pyrophosphohydrolase in B. subtilis.
DOI:doi:10.1074/jbc.RA119.011485
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1074/jbc.RA119.011485
 Verlag: http://www.jbc.org/content/294/52/19967
 DOI: https://doi.org/10.1074/jbc.RA119.011485
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:manganese
 metalloenzyme
 nucleic acid enzymology
 Nudix hydrolase
 pyrophosphohydrolase
 ribonucleolytic decay
 RNA degradation
 RNA processing
 RNA turnover
 YvcI
K10plus-PPN:1687622396
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68477532   QR-Code
zum Seitenanfang