The Experts below are selected from a list of 3603 Experts worldwide ranked by ideXlab platform
Yufeng Tong - One of the best experts on this subject based on the ideXlab platform.
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architecture of the native major Royal Jelly protein 1 oligomer
Nature Communications, 2018Co-Authors: Wenli Tia, Yazhou Zhao, Xiaoming Fang, Huiyua Guo, Wenju Peng, Xiaofeng Xue, Yang Liu, Kai Wang, Yufeng TongAbstract:Honeybee caste development is nutritionally regulated by Royal Jelly (RJ). Major Royal Jelly protein 1 (MRJP1), the most abundant glycoprotein among soluble Royal Jelly proteins, plays pivotal roles in honeybee nutrition and larvae development, and exhibits broad pharmacological activities in humans. However, its structure has long remained unknown. Herein, we identify and report a 16-molecule architecture of native MRJP1 oligomer containing four MRJP1, four apisimin, and eight unanticipated 24-methylenecholesterol molecules at 2.65 A resolution. MRJP1 has a unique six-bladed β-propeller fold with three disulfide bonds, and it interacts with apisimin mainly by hydrophobic interaction. Every four 24-methylenecholesterol molecules are packaged by two MRJP1 and two apisimin molecules. This assembly dimerizes to form an H-shaped MRJP14-apisimin4-24-methylenecholesterol8 complex via apisimin in a conserved and pH-dependent fashion. Our findings offer a structural basis for understanding the pharmacological effects of MRJPs and 24-methylenecholesterol, and provide insights into their unique physiological roles in bees.
Takanori Moriyama - One of the best experts on this subject based on the ideXlab platform.
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molecular characteristics and physiological functions of major Royal Jelly protein 1 oligomer
Proteomics, 2009Co-Authors: Shougo Tamura, Shizuka Amano, Toru Kono, Ju Kondoh, Kikuji Yamaguchi, Seiichi Kobayashi, Tokiyoshi Ayabe, Takanori MoriyamaAbstract:Royal Jelly contains numerous components, including proteins. Major Royal Jelly protein (MRJP) 1 is the most abundant protein among the soluble Royal Jelly proteins. In its physiological state, MRJP 1 exists as a monomer and/or oligomer. This study focuses the molecular characteristics and functions of MRJP 1 oligomer. MRJP 1 oligomer purified using HPLC techniques was subjected to the following analyses. The molecular weight of MRJP 1 oligomer was found to be 290 kDa using blue native-PAGE. MRJP 1 oligomer was separated into 55 and 5 kDa spots on 2-D blue native/SDS-PAGE. The 55 kDa protein was identified as MRJP 1 monomer by proteome analysis, whereas the 5 kDa protein was identified as Apisimin by N-terminal amino acid sequencing, and this protein may function as a subunit-joining protein within MRJP 1 oligomer. We also found that the oligomeric form included noncovalent bonds and was stable under heat treatment at 56 degrees C. Furthermore, MRJP 1 oligomer dose dependently enhanced and sustained cell proliferation in the human lymphoid cell line Jurkat. In conclusion, MRJP 1 oligomer is a heat-resistant protein comprising MRJP 1 monomer and Apisimin, and has cell proliferation activity. These findings will contribute to further studies analyzing the effects of MRJP 1 in humans.
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estimation and characterisation of major Royal Jelly proteins obtained from the honeybee apis merifera
Food Chemistry, 2009Co-Authors: Shougo Tamura, Toru Kono, Kikuji Yamaguchi, Chika Harada, Takanori MoriyamaAbstract:Abstract Royal Jelly (RJ) contains many components, including proteins. We focused on major Royal Jelly proteins (MRJPs) under natural conditions, and attempted to determine the content ratios and molecular forms of MRJPs by size-exclusion HPLC, SDS–PAGE, 2-DE and MALDI TOF/TOF MS. Soluble RJ proteins were extracted by dialysis followed by several centrifugation techniques. Soluble RJ proteins were universally separated into five peaks (640 kDa, 280 kDa, 100 kDa, 72 kDa and 4.5 kDa) by size-exclusion HPLC on a Superose 12 column. Among these peaks, both the 280 kDa and 72 kDa peaks were major, but the intensity of the 280 kDa peak differed markedly among original RJ samples ( n = 70). The main 280 kDa protein was separated into a 55 kDa band by reducing and non-reducing SDS–PAGE. This protein was also separated into multiple spots ranging from pH 4.2 to 6.5 by 2-DE. These spots were identified as MRJP 1 by MALDI TOF/TOF MS. From these results, MRJP 1 was thought to comprise an oligomer complex linked by non-covalent bonds under natural conditions. Another major protein, the 72 kDa peak on Superose 12 HPLC, was identified as MRJP 2.
Shougo Tamura - One of the best experts on this subject based on the ideXlab platform.
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molecular characteristics and physiological functions of major Royal Jelly protein 1 oligomer
Proteomics, 2009Co-Authors: Shougo Tamura, Shizuka Amano, Toru Kono, Ju Kondoh, Kikuji Yamaguchi, Seiichi Kobayashi, Tokiyoshi Ayabe, Takanori MoriyamaAbstract:Royal Jelly contains numerous components, including proteins. Major Royal Jelly protein (MRJP) 1 is the most abundant protein among the soluble Royal Jelly proteins. In its physiological state, MRJP 1 exists as a monomer and/or oligomer. This study focuses the molecular characteristics and functions of MRJP 1 oligomer. MRJP 1 oligomer purified using HPLC techniques was subjected to the following analyses. The molecular weight of MRJP 1 oligomer was found to be 290 kDa using blue native-PAGE. MRJP 1 oligomer was separated into 55 and 5 kDa spots on 2-D blue native/SDS-PAGE. The 55 kDa protein was identified as MRJP 1 monomer by proteome analysis, whereas the 5 kDa protein was identified as Apisimin by N-terminal amino acid sequencing, and this protein may function as a subunit-joining protein within MRJP 1 oligomer. We also found that the oligomeric form included noncovalent bonds and was stable under heat treatment at 56 degrees C. Furthermore, MRJP 1 oligomer dose dependently enhanced and sustained cell proliferation in the human lymphoid cell line Jurkat. In conclusion, MRJP 1 oligomer is a heat-resistant protein comprising MRJP 1 monomer and Apisimin, and has cell proliferation activity. These findings will contribute to further studies analyzing the effects of MRJP 1 in humans.
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estimation and characterisation of major Royal Jelly proteins obtained from the honeybee apis merifera
Food Chemistry, 2009Co-Authors: Shougo Tamura, Toru Kono, Kikuji Yamaguchi, Chika Harada, Takanori MoriyamaAbstract:Abstract Royal Jelly (RJ) contains many components, including proteins. We focused on major Royal Jelly proteins (MRJPs) under natural conditions, and attempted to determine the content ratios and molecular forms of MRJPs by size-exclusion HPLC, SDS–PAGE, 2-DE and MALDI TOF/TOF MS. Soluble RJ proteins were extracted by dialysis followed by several centrifugation techniques. Soluble RJ proteins were universally separated into five peaks (640 kDa, 280 kDa, 100 kDa, 72 kDa and 4.5 kDa) by size-exclusion HPLC on a Superose 12 column. Among these peaks, both the 280 kDa and 72 kDa peaks were major, but the intensity of the 280 kDa peak differed markedly among original RJ samples ( n = 70). The main 280 kDa protein was separated into a 55 kDa band by reducing and non-reducing SDS–PAGE. This protein was also separated into multiple spots ranging from pH 4.2 to 6.5 by 2-DE. These spots were identified as MRJP 1 by MALDI TOF/TOF MS. From these results, MRJP 1 was thought to comprise an oligomer complex linked by non-covalent bonds under natural conditions. Another major protein, the 72 kDa peak on Superose 12 HPLC, was identified as MRJP 2.
Eric A Miska - One of the best experts on this subject based on the ideXlab platform.
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a secreted rna binding protein forms rna stabilizing granules in the honeybee Royal Jelly
Molecular Cell, 2019Co-Authors: Eyal Maori, Isabela Cunha Navarro, Humberto F Oncristiani, David J Seilly, Konrad L M Rudolph, Alexandra Sapetschnig, Joh E Ladbury, Jay D Evans, Jonatha L Heeney, Eric A MiskaAbstract:Summary RNA flow between organisms has been documented within and among different kingdoms of life. Recently, we demonstrated horizontal RNA transfer between honeybees involving secretion and ingestion of worker and Royal jellies. However, how the Jelly facilitates transfer of RNA is still unknown. Here, we show that worker and Royal jellies harbor robust RNA-binding activity. We report that a highly abundant Jelly component, major Royal Jelly protein 3 (MRJP-3), acts as an extracellular non-sequence-specific RNA-aggregating factor. Multivalent RNA binding stimulates higher-order assembly of MRJP-3 into extracellular ribonucleoprotein granules that protect RNA from degradation and enhance RNA bioavailability. These findings reveal that honeybees have evolved a secreted dietary RNA-binding factor to concentrate, stabilize, and share RNA among individuals. Our work identifies high-order ribonucleoprotein assemblies with functions outside cells and organisms.
Jozef Simuth - One of the best experts on this subject based on the ideXlab platform.
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towards functional proteomics of minority component of honeybee Royal Jelly the effect of post translational modifications on the antimicrobial activity of apalbumin2
Proteomics, 2009Co-Authors: Katarina Ilikova, Ekaterina Mirgorodskaya, Gabriela Ukovska, Joha Gobom, Hans Lehrach, Jozef SimuthAbstract:This study illustrates multifunctionality of proteins of honeybee Royal Jelly (RJ) and how their neofunctionalization result from various PTMs of maternal proteins. Major proteins of RJ, designated as apalbumins belong to a protein family consisting of nine members with Mr of 49–87 kDa and they are accompanied by high number of minority homologs derived from maternal apalbumins. In spite of many data on diversity of apalbumins, the molecular study of their individual minority homologous is still missing. This work is a contribution to functional proteomics of second most abundant protein of RJ apalbumin2 (Mr 52.7 kDa). We have purified a minority protein from RJ; named as apalbumin2a, differ from apalbumin2 in Mr (48.6 kDa), in N-terminal amino acids sequences – ENSPRN and in N-linked glycans. Characterization of apalbumin2a by LC-MALDI TOF/TOF MS revealed that it is a minority homolog of the major basic Royal Jelly protein, apalbumin2, carrying two fully occupied N-glycosylation sites, one with high-mannose structure, HexNAc2Hex9, and another carrying complex type antennary structures, HexNAc4Hex3 and HexNAc5Hex4. We have found that apalbumin2a inhibit growth of Paenibacillus larvae. The obtained data call attention to functional plasticity of RJ proteins with potential impact on functional proteomics in medicine.
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apisimin a new serine valine rich peptide from honeybee apis mellifera l Royal Jelly purification and molecular characterization
FEBS Letters, 2002Co-Authors: K Ilikova, Jaroslav Klaudiny, J Hanes, E Nordhoff, Wolfram Saenge, Jozef SimuthAbstract:A peptide named apisimin was found in honeybee (Apis mellifera L.) Royal Jelly (RJ). N-terminal sequencing showed that this peptide corresponded to the sequence of a cDNA clone isolated from an expression cDNA library prepared from heads of nurse honeybees. No homology was found between the protein sequence of apisimin with a molecular mass of 5540.4 Da and sequences deposited in the Swiss-Prot database. The 54 amino acids of apisimin do not include Cys, Met, Pro, Arg, His, Tyr, and Trp residues. The peptide shows a well-defined secondary structure as observed by CD spectroscopy, and has the tendency to form oligomers. Isoelectrofocusing showed apisimin to be an acidic peptide.
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a family of major Royal Jelly proteins of the honeybee apis mellifera l
Cellular and Molecular Life Sciences, 1998Co-Authors: Jana Schmitzova, Jaroslav Klaudiny, Stefa Albe, W Schrode, W Schreckengos, J Hanes, J Judova, Jozef SimuthAbstract:The characterization of major proteins of honeybee larval Jelly (49 – 87 kDa) was performed by the sequencing of new complementary DNAs (cDNAs) obtained from a honeybee head cDNA library, by the determination of N-terminal sequences of the proteins, and by analyses of the newly obtained and known sequence data concerning the proteins. It was found that Royal Jelly (RJ) and worker Jelly (WJ) contain identical major proteins and that all the proteins belong to one protein family designated MRJP (from major Royal Jelly proteins). The family consists of five main members (MRJP1, MRJP2, MRJP3, MRJP4, MRJP5). The proteins MRJP3 and MRJP5 are polymorphic. MRJPs account for 82 to 90% of total larval Jelly protein, and they contain a relatively high amount of essential amino acids. These findings support the idea that MRJPs play an important role in honeybee nutrition.
