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DC Field | Value | Language |
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dc.contributor.author | Sainsbury, S | - |
dc.contributor.author | Lane, LA | - |
dc.contributor.author | Ren, J | - |
dc.contributor.author | Gilbert, RJ | - |
dc.contributor.author | Saunders, NJ | - |
dc.contributor.author | Robinson, CV | - |
dc.contributor.author | Stuart, DI | - |
dc.contributor.author | Owens, RJ | - |
dc.date.accessioned | 2012-09-14T14:53:13Z | - |
dc.date.available | 2012-09-14T14:53:13Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Nucleic Acids Research, 37(14): 4545 - 4558, Aug 2009 | en_US |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2724274/ | en |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/6664 | - |
dc.description | This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited - Copyright @ 2009 The Author(s). | en_US |
dc.description.abstract | LysR-type transcriptional regulators (LTTRs) form the largest family of bacterial regulators acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes. The LTTR, CrgA, from the human pathogen Neisseria meningitidis, is upregulated during bacterial–host cell contact. Here, we report the crystal structures of both regulatory domain and full-length CrgA, the first of a novel subclass of LTTRs that form octameric rings. Non-denaturing mass spectrometry analysis and analytical ultracentrifugation established that the octameric form of CrgA is the predominant species in solution in both the presence and absence of an oligonucleotide encompassing the CrgA-binding sequence. Furthermore, analysis of the isolated CrgA–DNA complex by mass spectrometry showed stabilization of a double octamer species upon DNA binding. Based on the observed structure and the mass spectrometry findings, a model is proposed in which a hexadecameric array of two CrgA oligomers binds to its DNA target site. | en_US |
dc.description.sponsorship | This study is funded by the UK Medical Research Council and the Biotechnology Biological Research Council; MRC Research Studentship; EPSRC/RSC Analytical Chemistry Trust Fund studentship. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Oxford University Press | en_US |
dc.title | The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators | en_US |
dc.type | Article | en_US |
dc.identifier.doi | http://dx.doi.org/10.1093/nar/gkp445 | - |
pubs.organisational-data | /Brunel | - |
pubs.organisational-data | /Brunel/Brunel Active Staff | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care/Biological Sciences | - |
pubs.organisational-data | /Brunel/Group Publication Pages | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups/Centre for Systems and Synthetic Biology | - |
Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers |
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Fulltext.pdf | 26.7 MB | Adobe PDF | View/Open |
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