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Conservation of MAP kinase activity and MSP genes in parthenogenetic nematodes

DOI: 10.1186/1471-213x-10-51

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Abstract:

We investigated two key elements of oocyte-to-embryo transition, MSP expression and MAP kinase signaling, in two parthenogenetic nematodes and their close hermaphroditic relatives. While activated MAP kinase is present in all analysed nematodes irrespective of the reproductive mode, MSP expression differs. In contrast to hermaphroditic or bisexual species, we do not find MSP expression at the protein level in parthenogenetic nematodes. However, genomic sequence analysis indicates that functional MSP genes are present in several parthenogenetic species.We present three alternative interpretations to explain our findings. (1) MSP has lost its function as a trigger of MAP kinase activation and is not expressed in parthenogenetic nematodes. Activation of the MAP kinase pathway is achieved by another, unknown mechanism. Functional MSP genes are required for occasionally emerging males found in some parthenogenetic species. (2) Because of long-term disadvantages, parthenogenesis is of recent origin. MSP genes remained intact during this short intervall although they are useless. As in the first scenario, an unknown mechanism is responsible for MAP kinase activation. (3) The molecular machinery regulating oocyte-to-embryo transition in parthenogenetic nematodes is conserved with respect to C. elegans, thus requiring intact MSP genes. However, MSP expression has been shifted to non-sperm cells and is reduced below the detection limits, but is still sufficient to trigger MAP kinase activation and embryogenesis.Throughout the animal kingdom, female gametes interrupt their development during oogenesis at various stages of meiosis. In response to external stimuli, this arrest is released, and oocyte maturation can take place. Then oocytes resume meiotic divisions, ovulate and get competent for fertilisation.An important step during oocyte maturation of all animals is MAP kinase activation (reviewed in [1-3]). MAP kinases are ubiquitous serine-threonine protein kinases expressed

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