Anti-Human BNC1 (a.a. 1-100) Polyclonal antibody

Basonuclin (BNC1), a zinc finger transcriptional factor, is essential for mouse spermatogenesis. However, the regulatory mechanisms of BNC1 in spermatogenesis are poorly understood. In this study, we identified HSF2BP, a testis-specific binding protein of HSF2, as a binding partner of BNC1 by using yeast two-hybrid screening. HSF2BP could interact with and inhibit BNC1 transcriptional activity without affecting its expression level. Moreover, coexpression of HSF2BP with BNC1 resulted in a striking redistribution of BNC1 to the cytoplasm. These data suggest that HSF2BP may play a pivotal role in regulating BNC1 transcriptional activity and subcellular localization during spermatogenesis. Structured summary of protein interactions: Bnc1 physically interacts with HSF2BP by two hybrid (View interaction) Bnc1 and HSF2BP colocalize by fluorescence microscopy (View interaction) Bnc1 physically interacts with HSF2BP by anti tag coimmunoprecipitation (View Interaction: 1, 2) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

The synthetic chelating agent EDTA can mobilize radionuclides and heavy metals in the environment. Biodegradation of EDTA should reduce this mobilization. Although several bacteria have been reported to mineralize EDTA, little is known about the biochemistry of EDTA degradation. Understanding the biochemistry will facilitate the removal of EDTA from the environment. EDTA-degrading activities were detected in cell extracts of bacterium BNC1 when flavin mononucleotide (FMN), NADH, and O-2 were present. The degradative enzyme system was separated into two different enzymes, EDTA monooxygenase and an FMN reductase, EDTA monooxygenase oxidized EDTA to glyoxylate and ethylenediaminetriacetate (ED3A), with the coconsumption of FMNH2 and O-2. The FMN reductase provided EDTA monooxygenase with FMNH2 by reducing FMN with NADH, The FMN reductase was successfully substituted in the assay mixture by other FMN reductases. EDTA monooxygenase was purified to greater than 95% homogeneity and had a single polypeptide with a molecular weight of 45,000, The enzyme oxidized both EDTA complexed with various metal ions and uncomplexed EDTA, The optimal conditions for activity were pH 7.8 and 35 degrees C. K(m)s were 34.1 mu M for uncomplexed EDTA and 8.5 mu M for MgEDTA(2-); this difference in K-m indicates that the enzyme has greater affinity for MgEDTA(2-). The enzyme also catalyzed the release of glyoxylate from nitrilotriacetate and diethylenetriaminepentaacetate. EDTA monooxygenase belongs to a small group of FMNH2-utilizing monooxygenases that attack carbon-nitrogen, carbon-sulfur, and carbon-carbon double bonds.