Signaling in the living systems : gene keys and gene locks

  • B. A. Kurchii P. H. E. I. “European University”, Ukraine, 03115, Kyiv, Akademika Vernadskyi Blvd., 16 V
Keywords: nucleosome, chromosome, histones, gene keys, gene lock

Abstract

This article briefly discusses the complex and intricate mechanisms of the functioning of signaling systems between the plasma membrane and the nucleus in the living organisms. An alternative model of DNA packaging is described. The milestone of this model is assumption that DNA winds not around the histone octamer: it is organized between two layers of nucleosomes. The basic structure of chromosomes is a triplet of nucleosomes. A single nucleosome is a parallelepiped in shape (11x11x6 nm). An alternative to protein receptors is proposed receptors composed from nucleic acid (DNA, RNA), called gene keys, that open the code (gene lock) of gene/cluster at the promoter.

References

Kurchii B. A. Signaling molecules can be presented by linear molecules of DNA: An alternative view. In: 5th Parnas Conference "Molecular mechanisms of cellular signaling", 25–29 April, 2005, Kyiv (Ukraine). Ukr Biokhim Zhurnal 2005. Vol. 77 (2) (Special issue). P. 197.

Kornberg R. D., Lorch Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell. 1999. Vol. 98. P. 285–294.

Alberts B., Johnson A., Lewis J., Raff M., Roberts K., Walter P. Molecular biology of the cell, 5th edn. New York : Garland Science, Taylor & Francis Group LLC, 2008. 1616 p.

Lewin B. Genes IX. Jones and Bartlett publishers, Inc, 2008.

Kurchii B. A. The three-dimensional architecture of chromatin: zigzag-shaped band of DNA is disposed between two layers of nucleosomes forming a chromosome. Ukr Bioorg Acta. 2004. Vol. 1 (No. 1). P. 67–73.

Kurchii B. A. What regulate the growth regulators? Second Edition, Revised and Expanded. Kyiv : Logos, 2019. 209 p.

Berg J. M., Tymoczko J. L., Stryer L. Biochemistry. 5th edn. New York: W H Freeman; 2002. Section 3.2, Primary structure: Amino acids are linked by peptide bonds to form polypeptide chains. Retrieved from: https://www.ncbi.nlm.nih.gov/books/NBK22364.

Allen F. H., Bird C.M., Rowland R.S., Raithby P.R. Hydrogen-bond acceptor and donor properties of divalent sulfur (Y-S-Z and R-S-H). Acta Cryst B53. 1997. P. 696–701. doi: 10.1107/S0108768197002644

Silerberg M. S. Chemistry. The molecular nature of matter and change. 4th edn. The McGrow-Hill Companies, 2006. 1264 p.

Cole H. A., Cui F., Ocampo J., Burke T. L., Nikitina T., Nagarajavel V., Kotomura N., Zhurkin V. B., Clark D. J. Novel nucleosomal particles containing core histones and linker DNA but no histone H1. Nucleic Acids Res. 2016. Vol. 44. P. 573–581. doi: 10.1093/nar/gkv943

Poonperm R., Takata H., Hamano T., Matsuda A., Uchiyama S., Hiraoka Y., Fukui K. Chromosome scaffold is a doublestranded assembly of scaffold proteins. Sci Reports. 2015. Vol. 5. P. 11916. doi: 10.1038/srep11916

Burgess R. J., Zhang Z. Histone chaperones in nucleosome assembly and human disease. Nat Struct Mol Biol. 2013. Vol. 20. P. 14–22. doi: 10.1038/nsmb.2461

Luger K., Mäder A. W., Richmond R. K., Sargent D. F., Richmond T. J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 1997. Vol. 389. P. 251–260. doi: 10.1038/38444