Corrinoid activation by a RACE protein: studies on the interaction of the proteins involved. Issue 1 (3rd June 2013)

• Record Type: Journal Article
• Authors: Nguyen, Hai Dang; Studenik, Sandra; Diekert, Gabriele
• Is Part Of: FEMS microbiology letters. Volume 345:Issue 1(2013:Aug.)
• Page Start: 31
• Page End: 38
• Publication Date: 2013-06-03
• Subjects: Microbiology -- Periodicals; 579
• DOI: 10.1111/1574-6968.12178
• Languages: English
• ISSNs: 0378-1097

Abstract

<abstract abstract-type="main" id="fml12178-abs-0001"> <title>Abstract</title> <p>The <italic>O</italic>‐demethylases of anaerobes are corrinoid‐dependent, ether‐cleaving methyltransferase enzyme systems consisting of four components. The interaction of the <italic>O</italic>‐demethylase components of the acetogenic bacterium <italic>Acetobacterium dehalogenans</italic> was studied by protein mobility on native PAGE, far‐Western blot analysis and yeast two‐hybrid screen. Using native PAGE and far‐Western blot, the interaction of the activating enzyme (AE) with its substrate, the corrinoid protein (CP), could be observed. The interaction occurred with four different CPs of <italic>A. dehalogenans</italic> and a CP from <italic>Desulfitobacterium hafniense </italic>DCB‐2, all involved in ether cleavage. In the corrinoid reduction assay, the AE reduced all CPs tested. This result indicates a broad substrate specificity of the AE of <italic>A. dehalogenans</italic>. In addition, an interaction of the <italic>A. dehalogenans</italic> CP of the vanillate‐<italic>O</italic>‐demethylase with the two methyltransferases of the same enzyme system was observed. The interaction of the ether‐cleaving methyltransferase with the CP appeared to be significantly less pronounced than that reported for the homologous methanol and methylamine methyltransferase systems of methanogenic archaea.</p> </abstract>