Article,

Molecular and biochemical characterization of the major royal jelly protein in bumblebees suggest a non-nutritive function

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Insect Biochemistry and Molecular Biology, 42 (9): 647 - 654 (2012)
DOI: https://doi.org/10.1016/j.ibmb.2012.05.003

Abstract

Honeybee queens are generated on purpose by extensive feeding with a glandular secretion termed royal jelly. Major royal jelly proteins (MRJPs) are the dominant proteinaceous component of royal jelly. One of them, MRJP1, was found to play a central role in honeybee queen development. Genes encoding \MRJPs\ were reported to originate from a single originator, and several of them have evolved nutritive function. Phylogenetic analysis provides evidence that the same originator has multiplied independently in Nasonia and ant lineages. Here we show that bumblebees represent a transition species preserving a single-copy pre-multiplication stage of \MRJP\ evolution. By exploring the single-copy BtRJPL gene, we found striking similarities with \MRJPs\ of the honeybee such as gene structure and expression regulation. At the same time it turned out that BtRJPL does not fulfill criteria for functioning as a nutritive protein. Instead we found evidence that BtRJPL is involved in food digestion or modification, which appears to be the original \MRJP\ function, at least in this lineage. Thus, the evolutionary pattern of \MRJPs\ in hymenopterans constitutes an excellent example of a functional diversification combined with the origin of new properties followed by intensive gene duplication events.

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