Towards posttranslational modification proteome of royal jelly
文献类型: 外文期刊
第一作者: Zhang, Lan
作者: Zhang, Lan;Fang, Yu;Li, Rongli;Feng, Mao;Han, Bin;Zhou, Tiane;Li, Jianke
作者机构:
关键词: Posttranslational modification;Royal jelly;Shotgun;Tandem mass spectrometry;Two-dimensional gel electrophoresis
期刊名称:JOURNAL OF PROTEOMICS ( 影响因子:4.044; 五年影响因子:4.02 )
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年卷期:
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收录情况: SCI
摘要: 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.
分类号: Q51
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