Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of putative promoters and genomic structure of mrjp1, the gene coding for the most abundant protein of larval food

Malecová, Barbora; Ramser, Juliane; O’Brien, John; Janitz, Michael; Judova, Jana; Lehrach, Hans; Šimúth, Jozef

doi:10.1016/s0378-1119(02)01174-5

Cited by 35 publications

(41 citation statements)

References 34 publications

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“…Genes coding for AmMRJPs are present as the single copy gene per haploid genome (Malecova et al, 2003). Bilikova et al (1999) illustrated that the single protein band of purified AmMRJP2, as analyzed by SDS-PAGE, was composed of at least 8 different isoelectric focusing variants of pI 7.5-8.5.…”

Section: Resultsmentioning

confidence: 99%

Cloning, Expression and Genomic Organization of Genes Encoding Major Royal Jelly Protein 1 and 2 of the Honey Bee (Apis cerana)

Imjongjirak¹,

Klinbunga²,

Sittipraneed³

2005

BMB Reports

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Section: Resultsmentioning

confidence: 99%

Cloning, Expression and Genomic Organization of Genes Encoding Major Royal Jelly Protein 1 and 2 of the Honey Bee (Apis cerana)

Imjongjirak¹,

Klinbunga²,

Sittipraneed³

2005

BMB Reports

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“…RJ contains 12%-15% protein, of which 80% belongs to soluble RJ proteins, the major RJ protein (MRJP) family (Howe et al, 1985;Simúth, 2001). Nine members of MRJP (MRJP1-9) have been reported; among them five (MRJP1-5) make up 82% of the total RJ protein content (Schmitzová et al, 1998;Malecová et al, 2003;Albert and Klaudiny, 2004;Drapeau et al, 2006;Shen et al, 2010b). MRJP1, designated as apalbumin 1, constitutes 45% of water-soluble proteins and is the most abundant protein in RJ (Furusawa et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Shen

Wang

Zhai

et al. 2015

J. Zhejiang Univ. Sci. B

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Major royal jelly protein 1 (MRJP1), designated apalbumin 1, has been regarded as a freshness marker of royal jelly (RJ). A MRJP1-specific peptide (IKEALPHVPIFD) identified by bioinformatics analysis of homologous members of the major royal protein family was synthesized and used to raise polyclonal anti-MRJP1 antibody (anti-SP-MRJP1 antibody). Western blot analysis showed that anti-SP-MRJP1 antibody only reacted with MRJP1 in RJ. In contrast, the previously reported antibody against recombinant MRJP1 (anti-R-MRJP1 antibody) reacted with other members of MRJP family in RJ. Enzyme-linked immunosorbent assay (ELISA) using anti-SP-MRJP1 antibody demonstrated that MRJP1 content in RJ stored at 40 °C significantly degraded by 37.3%, 55.9%, 58.0%, 60.6%, 65.7%, 72.7%, and 73.1% at 7, 14, 21, 28, 35, 42, and 49 d, respectively, when compared with MRJP1 content in fresh RJ (0 d). Optical density analysis of MRJP bands from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles demonstrated that the degradation of MRJP1, MRJP2, MRJP3, and MRJP5 in RJ was strongly and positively correlated with the period of storage (P<0.0001). Our results indicated anti-SP-MRJP1 antibody was highly specific for MRJP1, and ELISA using the antibody is a sensitive and easy-to-use method to determine the freshness and authenticity of RJ.

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“…Additionally, apalbumin 3, with its five isoforms, and apalbumin 2, seem to function as a store of processable form of nitrogen [34]. Apalbumin 1 [35,36], shows a mass of 55 kDa and self-assembling properties. In addition to nutrition function, this protein could also play a role in processing honey-bee products, in particular it may participate in the formation of pollen-pellet and pollen-bread [35].…”

Section: Introductionmentioning

confidence: 99%

“…Apalbumin 1, representing 48% of water soluble proteins of RJ, has been found also in honey, in the honey-bee pollenpellet and in the honey-bee pollen-bread. Its mRNA has been found expressed in the mushroom bodies of the adult honeybee brain [37] and in the hypopharingeal glands of both nurse bees and foragers [18,36,38]. Apalbumin 1 has been investigated by using cDNA cloning, immunoblotting, SDS-PAGE and 2-DE electrophoresis [15,18,33,35].…”

Section: Introductionmentioning

confidence: 99%

Towards royal jelly proteome

et al. 2005

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The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome. Apalbumin 1 was also confirmed to be present in honey-bee pollen-bread where the presence of apalbumin 2 was also found. In addition several fragments of apalbumin 1 and apalbumin 3 were also found in RJ. These could be the result of protease activity other than that of serine-protease. This study is a contribution to the description of royal jelly proteome.

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Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of putative promoters and genomic structure of mrjp1, the gene coding for the most abundant protein of larval food

Cited by 35 publications

References 34 publications

Cloning, Expression and Genomic Organization of Genes Encoding Major Royal Jelly Protein 1 and 2 of the Honey Bee (Apis cerana)

Cloning, Expression and Genomic Organization of Genes Encoding Major Royal Jelly Protein 1 and 2 of the Honey Bee (Apis cerana)

Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Towards royal jelly proteome

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