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Author Topic: Darwin  (Read 13969 times)

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Re: Darwin
« Reply #165 on: July 26, 2018, 10:05:20 pm »
Agelbert NOTE: For those who are unfamilar with Histones, I am posting some info and a video to help make clear to you how absolutely essential they are to life. 

Histones are one of the specific proteins involved in cell division and cancer. Technically, the ball-like groups of histones are referred to as nucleosomes, but--for simplicity--the website will continue to refer to these groups as histones.

In more general terms, histones are the protein “balls” that DNA wraps around in order to help DNA coil itself and condense into a chromosome during interphase. In fact, the image of nucleosomes (groups of histones) strung along a strand of DNA is often referred to as the "Beads on a String" model.

In the image below, you can see the histones, drawn as gray spheres that attach to the DNA and each other as the DNA condenses into a chromosome that can be easily divided and transported during cell division.

We, however, are interested in just the histones, as pictured below:

The video below provides a good representation of what histones look like in the cell. The clip denotes the histones as groups of orange spheres wrapped in blue globular DNA. Courtesy of jccairs.


You read that part about cell division, but, leaving the cancer issue aside for the moment, Histones have other vital functions. You all know what an anti-histamine spray is. Certain types of Histones cause the release of histamines (vasodilators - relax blood vessel smooth muscles and make them leaky) which give you a runny nose. It is an immune system response to get rid of something your body does not want. An anti-histamine spray counteracts that. You may not like that runny nose, but keeping it from running may not help in getting rid of some bacterial or viral agent attacking you, so please keep that in mind.

You also should know about the Histone that sends histamines to your H3 receptors when you eat sweets (they are located throughout your body). When those H3 receptors get hit too often, they become sensitized and more and more histamines are required to make the H3 receptors work. What work is that? It's calling for insulin to process the sugar. Eating too much sugar triggers a massive amount of histamines towards the H3 receptors. When the H3 receptors get overtaxed over a number of years, the person develops Diabetes.

I apologize for being so brief, but the point I wish to make is that we cannot function without Histones and that all of their functions are extremely fine tuned and targeted. Histones are an irreducibly complex part of the eukaryotic cell (Eukaryotic means true=Eu - karyot=nucleus versus Prokaryotic=bacterial cells - Pro=before) design.

They are either all there or they do not work. In the case of cancer, they work too much, which is also not part of their function. All biological functions work inside a life band of "not too little" and "not too much" activity. It is ludicrous to claim that any organism had a non-functioning partial group of all the histones that just randomly mutated to be an extremely precisely targeted tool of cell division and the immune system. Without Histones (and several other irreducibly complex parts of the celluar anatomy and physiology that work in precise harmony), there is no life because there is no cell division, period.  The fact thar Eukaryotic Histones can continue to function with several deleterious mutations, contrary to what evolutionary theory had predicted, strengthens the hypothesis of a robust original design, even though evolutionists are trying to talk their way around this.

Smileys added by yours truly.


Molecular evolution predictions

Histone proteins cannot tolerate much change

Histones are proteins which serve as the hubs about which DNA is wrapped. They are highly similar across vastly different species which means they must have evolved early in evolutionary history. As one textbook explains, “The amino acid sequences of four histones are remarkably similar among distantly related species. … The similarity in sequence among histones from all eukaryotes indicates that they fold into very similar three-dimensional conformations, which were optimized for histone function early in evolution in a common ancestor of all modern eukaryotes.” (Lodish et. al., Section 9.5) And this high similarity among the histones also means they must not tolerate change very well, as another textbook explains: “Changes in amino acid sequence are evidently much more harmful for some proteins than for others. … virtually all amino acid changes are harmful in histone H4. We assume that individuals who carried such harmful mutations have been eliminated from the population by natural selection.” (Alberts et. al. 1994, 243)

So the evolutionary prediction is that in these histone proteins practically all changes are deleterious: “As might be expected from their fundamental role in DNA packaging, the histones are among the most highly conserved eucaryotic proteins. For example, the amino acid sequence of histone H4 from a pea and a cow differ at only at 2 of the 102 positions. This strong evolutionary conservation suggests that the functions of histones involve nearly all of their amino acids, so that a change in any position is deleterious to the cell.” (Alberts et. al. 2002, Chapter 4)

This prediction has also been given in popular presentations of the theory: “Virtually all mutations impair histone’s function, so almost none get through the filter of natural selection. The 103 amino acids in this protein are identical for nearly all plants and animals.” (Molecular Clocks: Proteins That Evolve at Different Rates)

But this prediction has turned out to be false. An early study suggested that one of the histone proteins could well tolerate many changes. (Agarwal and Behe) And later studies confirmed and expanded this finding: “despite the extremely well conserved nature of histone residues throughout different organisms, only a few mutations on the individual residues (including nonmodifiable sites) bring about prominent phenotypic defects.” (Kim et. al.)

Similarly another paper documented these contradictory results: “It is remarkable how many residues in these highly conserved proteins can be mutated and retain basic nucleosomal function. … The high level of sequence conservation of histone proteins across phyla suggests a fitness advantage of these particular amino acid sequences during evolution.  Yet comprehensive analysis indicates that many histone mutations have no recognized phenotype.” (Dai et. al.) In fact, even more surprising, many mutations actually raised the fitness level. (Dai et. al.)


Agarwal, S., M. Behe. 1996. “Non-conservative mutations are well tolerated in the globular region of yeast histone H4.” J Molecular Biology 255:401-411.

Alberts, Bruce., D. Bray, J. Lewis, M. Raff, K. Roberts, J. Watson. 1994. Molecular Biology of the Cell. 3d ed. New York: Garland Publishing.

Alberts, Bruce., A. Johnson, J. Lewis, et. al. 2002. Molecular Biology of the Cell. 4th ed. New York: Garland Publishing. http://www.ncbi.nlm.nih.gov/books/NBK26834/

Dai, J., E. Hyland, D. Yuan, H. Huang, J. Bader, J. Boeke. 2008. “Probing nucleosome function: a highly versatile library of synthetic histone H3 and H4 mutants.” Cell 134:1066-1078.

Kim, J., J. Hsu, M. Smith, C. Allis. 2012. “Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast.” Proceedings of the National Academy of Sciences 109:5779-5784.

Lodish H., A. Berk, S. Zipursky, et. al. 2000. Molecular Cell Biology. 4th ed. New York: W. H. Freeman. http://www.ncbi.nlm.nih.gov/books/NBK21500/

“Molecular Clocks: Proteins That Evolve at Different Rates.” 2001. WGBH Educational Foundation and Clear Blue Sky Productions.


Light is sown for the righteous, and gladness for the upright in heart. Ps. 97:11


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