ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

Article Abstract:

Research was conducted to test whether the ARF protein can stabilize the p53 protein by binding to and advocating the degradation of MDM2. HeLa cells were harvested after overnight culture while coupled in vitro transcription and translation procedures were performed utilizing the TNT kit. Results showed that the destabilization of MDM2 by ARF precluded the detection of in vivo complex formation between the two proteins. They also revealed a tumor suppression pathway that involved two tumor suppressors.

Physiological aspects, Tumor suppressor genes

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Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form

Article Abstract:

Three SoxRc proteins with alterations in various portions of the polypeptide are examined. The proteins contain (2Fe-2S) centers necessary for in vitro transcription and are inactivated by chemical reduction. The proteins failed to accumulate with reduced 2Fe-2S even without oxidative stress. Data support the hypothesis that oxidation of the SoxR (2Fe-2S) clusters is the instrument for sensing oxidative stress and activating the SoxR protein as a transcription factor.

Oxidation-reduction reaction, Oxidation-reduction reactions

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Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment

Article Abstract:

A study was conducted to characterize the three-dimensional caspase recruitment domain structure of RAIDD adaptor proteins using nuclear magnetic resonance (NMR) spectroscopy. Varian spectrometers were used to determine NMR spectra while structure computations were carried out based on simulated annealing protocols. Results indicated that the adaptor proteins support a six-helix bundle and distinct charged surface patches.

Usage, Nuclear magnetic resonance spectroscopy

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