Towards Posttranslational Modification Proteome of Royal Jelly
Journal of Proteomics, Volume 75, Issue 17, 18 September 2012, Pages 5327–5341
Royal jelly (RJ) is a secretory protein from the hypopharyngeal glands of nurse honeybee workers, which contains a variety of proteins of which major royal jelly proteins (MRJPs) are some of the most important. It plays important roles both for honeybee and human.
Each family of MRJP 1–5 displays a string of modified protein spots in the RJ proteome profile, which may be caused by posttranslational modifications (PTMs) of MRJPs. However, information on the RJ PTMs is still limited. Therefore, the PTM status of RJ was identified by using complementary proteome strategies of two-dimensional gel electrophoresis (2-DE), shotgun analysis in combination with high performance liquid chromatography-chip/electrospray ionization quadrupole time-of-flight/tandem mass spectrometry and bioinformatics. Phosphorylation was characterized in MRJP 1, MRJP 2 and apolipophorin-III-like protein for the first time and a new site was localized in venom protein 2 precursor. Methylation and deamidation were also identified in most of the MRJPs.
The results indicate that methylation is the most important PTM of MRJPs that triggers the polymorphism of MRJP 1–5 in the RJ proteome.
Our data provide a comprehensive catalog of several important PTMs in RJ and add valuable information towards assessing both the biological roles of these PTMs and deciphering the mechanisms underlying the beneficial effects of RJ for human health.
► Phosphorylation was found in four royal jelly (RJ) proteins. ► Methylation and deamidation were identified in most of major royal jelly proteins. ► Polymorphism of major royal jelly proteins is mainly caused by methylation. ► The results extend our knowledge on the biochemical natures of RJ.