Imperial College London
Portrait Picture

Professor José R Penadés

Faculty of Medicine, Department of Infectious Disease

Director MRC Centre for Molecular Bacteriology & Infection
 
 
 
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Contact

 

+44 (0)20 7594 8533j.penades Website

 
 
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Assistant

 

Mrs Anna Lee +44 (0)20 7594 2954

 
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Location

 

Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Maiques:2016:nar/gkw317,
author = {Maiques, E and Quiles-Puchalt, N and Donderis, J and Rafael, Ciges-Tomas J and Alite, C and Bowring, JZ and Humphrey, S and Penades, JR and Marina, A},
doi = {nar/gkw317},
journal = {Nucleic Acids Research},
pages = {5457--5469},
title = {Another look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party},
url = {http://dx.doi.org/10.1093/nar/gkw317},
volume = {44},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - We have recently proposed that the trimeric staphylococcal phage encoded dUTPases (Duts) are signaling molecules that act analogously to eukaryotic G-proteins, using dUTP as a second messenger. To perform this regulatory role, the Duts require their characteristic extra motif VI, present in all the staphylococcal phage coded trimeric Duts, as well as the strongly conserved Dut motif V. Recently, however, an alternative model involving Duts in the transfer of the staphylococcal islands (SaPIs) has been suggested, questioning the implication of motifs V and VI. Here, using state-of the-art techniques, we have revisited the proposed models. Our results confirm that the mechanism by which the Duts derepress the SaPI cycle depends on dUTP and involves both motifs V and VI, as we have previously proposed. Surprisingly, the conserved Dut motif IV is also implicated in SaPI derepression. However, and in agreement with the proposed alternative model, the dUTP inhibits rather than inducing the process, as we had initially proposed. In summary, our results clarify, validate and establish the mechanism by which the Duts perform regulatory functions.
AU  - Maiques,E
AU  - Quiles-Puchalt,N
AU  - Donderis,J
AU  - Rafael,Ciges-Tomas J
AU  - Alite,C
AU  - Bowring,JZ
AU  - Humphrey,S
AU  - Penades,JR
AU  - Marina,A
DO  - nar/gkw317
EP  - 5469
PY  - 2016///
SN  - 0305-1048
SP  - 5457
TI  - Another look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party
T2  - Nucleic Acids Research
UR  - http://dx.doi.org/10.1093/nar/gkw317
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000379753100049&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/80394
VL  - 44
ER  -
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