Erratum to: Structure of Chromatin in Spermatozoa

Abstract

The specialized structure of the sperm chromatin has a dual function – first to protect the DNA from damage during storage and transport to the oocyte, and then to enable a rapid and complete unpacking of the undamaged paternal genome in the ooplasm. It is evident that zinc has a pivotal role in maintaining the structural stability and in enabling a rapid decondensation at the appropriate time. It is important for the sperm chromatin structure that the spermatozoa are ejaculated together with the zinc-rich prostatic secretion. Early exposure to zinc-binding seminal vesicular fluid can deplete the sperm chromatin of zinc and most likely induce surplus formation of disulfide bridges, likely to cause incomplete and delayed decondensation of the sperm chromatin in the oocyte. A premature decrease in sperm chromatin structure stability is likely to increase the risk for damage to the DNA due to increased access to the genome for DNA damaging compounds. The status of the sperm chromatin structure can vary in vitro depending on the exposure to zinc-depleting conditions when spermatozoa are stored in semen after ejaculation. When sperm DNA damage tests are evaluated and validated, it is therefore essential to also take into account the dynamics of zinc-dependent and zinc-independent sperm chromatin stability.

The online version of the original chapter can be found at http://dx.doi.org/10.1007/978-1-4614-7783-9_12

The publisher regrets the following information was mistakenly interpreted on legend for Figure 1.1 during the production process. The correct legend is as follows:

Fig. 1.1 Schematic view of DNA double helix in sperm chromatin and its relation to protamine compounds, indicating possible role of zinc to connect protamines: one zinc per protamine molecule for every ten base pairs (turn of the helix) of the DNA. If negative charges of phosphate groups in DNA are neutralized by protamines, tight packing of sperm DNA chromatin fibers is possible. With permission from Björndahl and Kvist (2010)