Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum.

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Title: Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum.
Authors: Ostrowski, Adam1, Gundogdu, Mehmet1, Ferenbach, Andrew T.2, Lebedev, Andrey A.3, van Aalten, Daan M. F.1,2 vanaalten@dundee.ac.uk
Source: Journal of Biological Chemistry. 18/12/2015, Vol. 290 Issue 51, p30291-30305. 15p.
Subjects: Protein analysis, Metazoa, Thermophilic bacteria, Hydrolases, Transferase structure
Abstract: Background: ProteinO-GlcNAcylation is essential for function and stability of many proteins in metazoa and is essential for development. Results: Thermobaculum terrenum encodes a functional O-GlcNAc hydrolase and a conserved O-GlcNAc-transferase. Conclusion: T. terrenum is the first known bacterium to possess the components for a functional O-GlcNAc system. Significance: T. terrenum could become a reductionist model to study protein O-GlcNAcylation on an organism level. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum.
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 18/12/2015, Vol. 290 Issue 51, p30291-30305. 15p.
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  Data: <searchLink fieldCode="DE" term="%22Protein+analysis%22">Protein analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Metazoa%22">Metazoa</searchLink><br /><searchLink fieldCode="DE" term="%22Thermophilic+bacteria%22">Thermophilic bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrolases%22">Hydrolases</searchLink><br /><searchLink fieldCode="DE" term="%22Transferase+structure%22">Transferase structure</searchLink>
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  Data: Background: ProteinO-GlcNAcylation is essential for function and stability of many proteins in metazoa and is essential for development. Results: Thermobaculum terrenum encodes a functional O-GlcNAc hydrolase and a conserved O-GlcNAc-transferase. Conclusion: T. terrenum is the first known bacterium to possess the components for a functional O-GlcNAc system. Significance: T. terrenum could become a reductionist model to study protein O-GlcNAcylation on an organism level. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1074/jbc.M115.689596
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      – Code: eng
        Text: English
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        Type: general
      – SubjectFull: Metazoa
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      – SubjectFull: Thermophilic bacteria
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      – SubjectFull: Hydrolases
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      – SubjectFull: Transferase structure
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      – TitleFull: Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum.
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              Text: 18/12/2015
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