An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3

Article Abstract:

A study of the anti-oncogenic activity of Mxi1 helps define two mxi1 mRNAs that result from alternative RNA processing and code for proteins with varying potentials for the inhibition of myc-activated transformation. An amino-terminal extension of 36 residues in one of the two Mxi protein forms is associated with the potential for strong repressive activity. The yeast two-hybrid interaction system helps demonstrate that this highly conserved alpha-helical Mxi1 repression domain binds to a murine yeast transcriptional repressor SIN3 homolog. Mix1 and mouse Sin3 are part of a ternary complex, as revealed by coimmunoprecipitation studies in mammalian cells.

Genetic regulation, Genetic transcription, Transcription (Genetics), Yeast, Yeast (Food product), Proto-oncogenes

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Longevity, stress response, and cancer in aging telomerase-deficient mice

Article Abstract:

Telomeres play a vital role in maintaining cell viability and chromosomal activity. Telomeres are also believed to be involved in the signaling of cellular senescence, although no link with organismal aging has been proven. Telomerase null mice were generated and examined to explore the possible role of telomeres in aging. Results showed that loss of telomere function did not elicit any classical symptoms of aging. However, age-dependent telomere shortening was found to be linked with a shorter life span as well as a lessened ability to heal wounds.

Aging, Telomeres, Laboratory animals

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Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

Article Abstract:

The Max interactor 1 (Mxi1) protein is a novel human protein that was isolated using the interaction trap, a yeast genetic selection method. Mxi1 contains a basic-helix-loop-helix-Zip motif similar to that found to in the Myc protein family. In addition, it specifically interacts with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. In differentiation-inducible U-937 cells, expression ofMxi1 is elevated. These results indicate that Mxi1, as well as Mad, indirectly regulate c-Myc function by sequestering Max.

Ligand binding (Biochemistry), Tumor proteins

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