The protamine family of sperm nuclear proteins |
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Authors: | Rod Balhorn |
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Institution: | (1) Biosciences and BioTechnology Division, Chemistry, Materials and Life Sciences, Lawrence Livermore National Laboratory, East Avenue, Livermore, CA 94550, USA |
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Abstract: | The protamines are a diverse family of small arginine-rich proteins that are synthesized in the late-stage spermatids of many
animals and plants and bind to DNA, condensing the spermatid genome into a genetically inactive state. Vertebrates have from
one to 15 protamine genes per haploid genome, which are clustered together on the same chromosome. Comparison of protamine
gene and amino-acid sequences suggests that the family evolved from specialized histones through protamine-like proteins to
the true protamines. Structural elements present in all true protamines are a series of arginine-rich DNA-anchoring domains
(often containing a mixture of arginine and lysine residues in non-mammalian protamines) and multiple phosphorylation sites.
The two protamines found in mammals, P1 and P2, are the most widely studied. P1 packages sperm DNA in all mammals, whereas
protamine P2 is present only in the sperm of primates, many rodents and a subset of other placental mammals. P2, but not P1,
is synthesized as a precursor that undergoes proteolytic processing after binding to DNA and also binds a zinc atom, the function
of which is not known. P1 and P2 are phosphorylated soon after their synthesis, but after binding to DNA most of the phosphate
groups are removed and cysteine residues are oxidized, forming disulfide bridges that link the protamines together. Both P1
and P2 have been shown to be required for normal sperm function in primates and many rodents. |
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