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J. Biol. Chem. 283, 8014–8022. Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation. 2008

Muik, M., Frischauf, I., Derler, I., Fahrner, M., Bergsmann, J., Eder, P., Schindl, R., Hesch, C., Polzinger, B., Fritsch, R., Kahr, H., Madl, J., Gruber, H., Groschner, K. and Romanin, C.

Notes: The authors performed protein pull-down assays to characterize the interaction of ORAI1 and STIM1, two protein components of the calcium-release calcium current. His6-STIM1 C terminus and ORAI1 were synthesized using the TNT® Coupled Reticulocyte Lysate System in the presence of 35S, and His6-STIM1 C terminus was immobilized using MagZ™ Binding Particles. An aliquot of the TNT® reaction expressing ORAI1 was added to the particles, and proteins were washed, eluted using increasing concentrations of imidazole (10–40mM) and analyzed by SDS-PAGE. In a second set of pull-down assays, His6-STIM1 C terminus was used to pull down ORA1 N- and C-terminal fragments expressed as GST fusion proteins. The His6-STIM1 C terminus protein was purified from transiently tranfected HEK293 cells using the MagneHis™ Protein Purification System. (3781)

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Proc. Natl. Acad. Sci. USA 105, 12485–90. Selenoprotein N is required for ryanodine receptor calcium release channel activity in human and zebrafish muscle. 2008

Jurynec, M.J., Xia, R., Mackrill, J.J., Gunther, D., Crawford, T., Flanigan, K.M., Abramson, J.J., Howard, M.T and Grunwald, D.J.

Notes: The authors show that SepN, a selenoprotein of unknown function, and ryanodine receptor (RyR) intracellular calcium release channel are both required for normal muscle development in zebrafish. Furthermore SepN and RyR interact, and SepN is required for full activity of the RyR channel. As part of their study, the authors expressed SepN as a polyhistidine-tagged (8X His) protein in TNT® Coupled Reticulocyte Lysate System and purified it using the MagZ™ Protein Purification System. The TNT® reaction was modified to optimize selenocysteine incorporation efficiency; the reaction contained 80% rabbit reticulocyte lysate (RRL), 1mM methionine, 0.4mM spermidine, 0.01µg/ml SepN-8X-His DNA and 300nM of the C-terminus of Secis Binding Protein 2 , which is required for efficient incorporation of selenocysteine in RRL-based reactions. (3898)

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J. Biol. Chem. 282, 22575–22764. Allosteric activation of human glucokinase by free polyubiquitin chains and its ubiquitin-dependent cotranslational proteasomal degradation. 2007

Bjørkhaug, L., Molnes, J., Søvik, O., Njølstad, P.R. and Flatmark, T.

Notes: The authors identified human glucokinase (hGK) as a substrate for the ubiquitin-conjugating enzyme system of rabbit reticulocyte lysate (RRL). Wildtype hGK, His6-hGK and His6-hGK mutants were expressed in the TNT® T7 Quick Coupled Transcription/Translation System in the presence of [35S]methionine and 10µM ubiquitin (in additional to the endogenous ubiquitin in RRL). Ubiquitinated and polyubiquitinated proteins were detected as size-shifted bands by SDS-PAGE and by two-dimensional polacylamide electrophoresis followed by immunoblotting with an anti-ubiquitin antibody. For some experiments, His6-hGK and His6-hGK mutants were isolated using the MagZ™ Protein Purification System prior to ubiquitination. (3718)

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Genes Dev. 21, 1125–1138. Lin-28 binds IGF-2 mRNA and participates in skeletal myogenesis by increasing translation efficiency. 2007

Polesskaya, A., Cuvellier, S., Naguibneva, I., Duquet, A., Moss, E.G. and Harel-Bellan, A.

Notes: The protein Lin-28 is a translational enhancer in differentiating myoblasts; one target of Lin-28 is insulin-like growth factor 2 (IGF-2). The authors showed that Lin-28 increased expression of an IGF-2 reporter construct in vitro. [35S]-methionine-labeled, His-tagged Lin-28 was expressed in the TNT® Coupled Reticulocyte Lysate System and purified using the MagZ™ Protein Purification System. Increasing amounts of purified Lin-28 protein were added to a TNT® Coupled Reticulocyte Lysate System reaction containing an IGF-2 luciferase reporter vector, and as a result, luciferase expression was increased up to threefold. Experiments performed with an irrelevant His-tagged protein of equal size and with an equal number of methionine residues confirmed that the increase in luciferase activity was specific to Lin-28. Side-by-side experiments performed with a luciferase reporter vector without the IGF-2 regulatory element did not show increased luciferase activity. (3717)

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Cancer Res. 67, 455–464. NKX3.1 homeodomain protein binds to topoisomerase I and enhances its activity. 2007

Bowen, C., Stuart, A., Ju, J.H., Tuan, J., Blonder, J., Conrads, T.P., Veenstra, T.D. and Gelmann, E.P.

Notes: The authors confirmed the interaction of NKX3.1, a prostate-specific homeodomain protein, and topoisomerase I. To determine of this interaction was dependent upon nucleic acid, two types of pull-down assays were performed in the presence of DNase or RNase. For the GST pull-down assay, fragments of topoisomerase I were expressed as GST-fusion proteins, and NKX3.1 was expressed as an [35S]methionine-labeled protein in the TNT® Quick Coupled Transcription/Translation System. Equimolar amount of GST or GST-topoisomerase I, bound to glutathione sepharose beads, and NKK3.1 were precipitated . In addition, fragments of NKX3.1 were expressed as polyhistidine-tagged proteins and captured using the MagZ™ Binding Particles. Equal molar amounts of NKX3.1 and [35S]methionine-labeled topoisomerase were incubated to examine protein interaction. (3716)

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