Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection

Show simple item record Rosberg-Cody, Eva Liavonchanka, Alena Göbel, Cornelia Ross, R. Paul O'Sullivan, Orla Fitzgerald, Gerald F. Feussner, Ivo Stanton, Catherine 2012-12-12T12:05:57Z 2012-12-12T12:05:57Z 2011 2011-02-17
dc.identifier.citation Rosberg-Cody, E., Liavonchanka, A., Göbel, C., Ross, R.P., O'Sullivan, O., Fitzgerald, G.F., Feussner, I., Stanton, C., 2011. Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection. BMC Biochemistry 12(9). doi: 10.1186/1471-2091-12-9 en
dc.identifier.volume 12 en
dc.identifier.startpage 9 en
dc.identifier.issn 1471-2091
dc.identifier.doi 10.1186/1471-2091-12-9
dc.description.abstract Background: The aim of this study was to determine the catalytic activity and physiological role of myosin-crossreactive antigen (MCRA) from Bifidobacterium breve NCIMB 702258. MCRA from B. breve NCIMB 702258 was cloned, sequenced and expressed in heterologous hosts (Lactococcus and Corynebacterium) and the recombinant proteins assessed for enzymatic activity against fatty acid substrates. Results: MCRA catalysed the conversion of palmitoleic, oleic and linoleic acids to the corresponding 10-hydroxy fatty acids, but shorter chain fatty acids were not used as substrates, while the presence of trans-double bonds and double bonds beyond the position C12 abolished hydratase activity. The hydroxy fatty acids produced were not metabolised further. We also found that heterologous Lactococcus and Corynebacterium expressing MCRA accumulated increasing amounts of 10-HOA and 10-HOE in the culture medium. Furthermore, the heterologous cultures exhibited less sensitivity to heat and solvent stresses compared to corresponding controls. Conclusions: MCRA protein in B. breve can be classified as a FAD-containing double bond hydratase, within the carbon-oxygen lyase family, which may be catalysing the first step in conjugated linoleic acid (CLA) production, and this protein has an additional function in bacterial stress protection. en
dc.description.sponsorship Science Foundation Ireland (SFI-CSET); Science Foundation Ireland (02/CE/B 124); Science Foundation Ireland (07/CE/B1368); Irish Government (National Development Plan); European Commission (QLK1-2002-02362); Carl von Ossietzky Universität Oldenburg, Germany (Georg-Christoph-Lichtenberg Scholarship for PhD Program 'Molecular Biology') en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher BioMed Central en
dc.rights © 2011 Rosberg-Cody et al; licensee BioMed Central Ltd. en
dc.rights.uri en
dc.subject Myosin-cross-reactive antigen (MCRA) en
dc.subject Bifidobacterium breve en
dc.subject Fatty acid hydratase en
dc.subject Stress protection en
dc.subject Lactococcus en
dc.subject Corynebacterium en
dc.title Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection en
dc.type Article (peer-reviewed) en
dc.internal.authorurl en
dc.internal.authorcontactother Gerald F. Fitzgerald, Microbiology Department, University College Cork, Cork, Ireland. Email: en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.rssid 90194391
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Irish Government en
dc.contributor.funder European Commission en
dc.contributor.funder Carl von Ossietzky Universität Oldenburg, Germany de
dc.description.status Peer reviewed en
dc.identifier.journaltitle BMC Biochemistry en
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