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Cell division and renewal i.e. mitosis, is at the backbone of every antibody catalog, with antibodies to proteins controlling mitosis, such as histone H3, being widely used in areas such as cancer research and epigenetics. A recent antibody study threw exciting new light on the way in which histone H3 works.

The histone family comprise 4 proteins which, together, form the octamer around which DNA is tightly wrapped to form chromatin (i.e. the chromosome component within the nucleus.) The DNA and histone core together form the nucleosome. Gene expression is regulated by acetylation of the histone proteins. During DNA transcription, all 4 are highly modified. However, H3 undergoes the most radical post-translational changes, with variability in sequence and modification states thought to be important to gene regulation

Phospho-specific antibody studies have revealed that H3 is phosphorylated in prophase and dephosphorylated in the anaphase stages of mitosis. This is achieved by the addition of a phosphate group at the threonine 3 site (H3T3). Now, researchers at Rockefeller University have uncovered a link with Survivin, which also plays an essential role in mitosis.

Survivin is part of the CPC (chromosomal passenger complex) of proteins. Previous antibody studies have demonstrated that CPC is essential to cell division, migrating to the chromatin to facilitate spindle microtubule assembly via the enzyme Aurora B. The new study showed that H3 phosphorylation is recognised by a binding pocket in the BIR domain of Survivin. This was followed by CPC recruitment to the chromatin, and Aurora B activation.

Chromosome segregation was followed by modulation of the kinase activity of Haspin, the enzyme responsible for H3T3 phosphorylation. This caused defects in the Aurora B spindle assembly process, allowing rebundling of the chromosomes to take place.

We at Novus Biologicals have a wide range of products on our antibody database devoted to cancer research. Both Survivin and Aurora B have been implicated in cancer formation, as have the IAP (inhibitor of apoptosis) proteins. The mechanism for Survivin/H3T3 recognition and IAP ligand binding are remarkably similar.



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