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The common marmoset (Callithrix jacchus) has two very similar semenogelin genes as the result of gene conversion

Valtonen-André, Camilla LU ; Ceder, Yvonne LU ; Kullberg, Morgan LU ; Nayudu, Penelope L. and Lundwall, Åke LU (2007) In Biology of Reproduction 76(4). p.604-610
Abstract
The semen coagulum proteins have undergone substantial structural changes during evolution. In primates, these seminal vesicle-secreted proteins are known as semenogelin I (SEMG1) and semenogelin II (SEMG2). Previous studies on the common marmoset (Callithrix jacchus) showed that ejaculated semen from this New World monkey contains semenogelin, but it remained unclear whether it carries both genes or only SEMG1 and no SEMG2, like the closely related cotton-top tamarin (Saguinus oedipus). In this study we show that there are two genes, both expressed in the seminal vesicles. Surprisingly, the genes show an almost perfect sequence identity in a region of 1.25 kb, encompassing nearly half of the genes and containing exon 1, intron 1, and the... (More)
The semen coagulum proteins have undergone substantial structural changes during evolution. In primates, these seminal vesicle-secreted proteins are known as semenogelin I (SEMG1) and semenogelin II (SEMG2). Previous studies on the common marmoset (Callithrix jacchus) showed that ejaculated semen from this New World monkey contains semenogelin, but it remained unclear whether it carries both genes or only SEMG1 and no SEMG2, like the closely related cotton-top tamarin (Saguinus oedipus). In this study we show that there are two genes, both expressed in the seminal vesicles. Surprisingly, the genes show an almost perfect sequence identity in a region of 1.25 kb, encompassing nearly half of the genes and containing exon 1, intron 1, and the first 0.9 kb of exon 2. The underlying molecular mechanism is most likely gene conversion, and a phylogenetic analysis suggests that SEMG1 is the most probable donor gene. The marmoset SEMG1 in this report differs from a previously reported cDNA by a lack of nucleotides encoding one repeat of 60 amino acids, suggesting that marmoset SEMG1 displays allelic size variation. This is similar to what was recently demonstrated in humans, but in marmosets the polymorphism was generated by a repeat duplication, whereas in humans it was a deletion. Together, these studies shed new light on the evolution of semenogelins and the mechanisms that have generated the structural diversity of semen coagulum proteins. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
epididymis, seminal vesicles, sperm, male reproductive tract, motility and transport
in
Biology of Reproduction
volume
76
issue
4
pages
604 - 610
publisher
Oxford University Press
external identifiers
  • wos:000245092900008
  • scopus:33947515265
ISSN
1529-7268
DOI
10.1095/biolreprod.106.057661
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Department of Cell and Organism Biology (Closed 2011.) (011002100), Clinical Chemistry, Malmö (013016000)
id
0abac886-2c77-40a9-8012-a6706fd19f47 (old id 669946)
date added to LUP
2016-04-01 12:06:15
date last changed
2020-01-12 09:13:18
@article{0abac886-2c77-40a9-8012-a6706fd19f47,
  abstract     = {The semen coagulum proteins have undergone substantial structural changes during evolution. In primates, these seminal vesicle-secreted proteins are known as semenogelin I (SEMG1) and semenogelin II (SEMG2). Previous studies on the common marmoset (Callithrix jacchus) showed that ejaculated semen from this New World monkey contains semenogelin, but it remained unclear whether it carries both genes or only SEMG1 and no SEMG2, like the closely related cotton-top tamarin (Saguinus oedipus). In this study we show that there are two genes, both expressed in the seminal vesicles. Surprisingly, the genes show an almost perfect sequence identity in a region of 1.25 kb, encompassing nearly half of the genes and containing exon 1, intron 1, and the first 0.9 kb of exon 2. The underlying molecular mechanism is most likely gene conversion, and a phylogenetic analysis suggests that SEMG1 is the most probable donor gene. The marmoset SEMG1 in this report differs from a previously reported cDNA by a lack of nucleotides encoding one repeat of 60 amino acids, suggesting that marmoset SEMG1 displays allelic size variation. This is similar to what was recently demonstrated in humans, but in marmosets the polymorphism was generated by a repeat duplication, whereas in humans it was a deletion. Together, these studies shed new light on the evolution of semenogelins and the mechanisms that have generated the structural diversity of semen coagulum proteins.},
  author       = {Valtonen-André, Camilla and Ceder, Yvonne and Kullberg, Morgan and Nayudu, Penelope L. and Lundwall, Åke},
  issn         = {1529-7268},
  language     = {eng},
  number       = {4},
  pages        = {604--610},
  publisher    = {Oxford University Press},
  series       = {Biology of Reproduction},
  title        = {The common marmoset (Callithrix jacchus) has two very similar semenogelin genes as the result of gene conversion},
  url          = {http://dx.doi.org/10.1095/biolreprod.106.057661},
  doi          = {10.1095/biolreprod.106.057661},
  volume       = {76},
  year         = {2007},
}