Sequence of the Hexameric Juvenile Hormone-binding Protein from the Hemolymph of Locusta migratoria

Braun, Ralph; Wyatt, G.R.

doi:10.1074/jbc.271.49.31756

Cited by 88 publications

(66 citation statements)

References 42 publications

(44 reference statements)

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“…Strong evidence suggests that hexamerin-like proteins of terrestrial insects evolved from oxygen-carrying hemocyanins of ancestral aquatic insects and crustaceans (24,25). In terrestrial insects, the hexamerins have acquired diverse storage (26) and hormone-binding functions (19). Our data suggest a previously undescribed function for termite hexameric storage proteins, which classically occur at high levels during preimaginal stages in most other insects (26).…”

Section: Effects Of Rnai On Hexamerin Protein Expressionmentioning

confidence: 77%

“…First, based on the finding that a closely related locust hexamerin serves as a JH-binding protein (19), it is possible that the termite hexamerins are capable of JH sequestration. In agreement with this, we have observed that the Hex-1 protein is recognized by the anti-JH antiserum described by Goodman et al (31) and that immunoreactivity is reduced in the presence of competing JH and after stripping with apolar solvents (32).…”

Section: Effects Of Rnai On Hexamerin Protein Expressionmentioning

confidence: 99%

“…Using these tools, we previously identified two JH-responsive and morphogenesis-associated hexamerin genes that are referred to as Hex-1 and Hex-2 (6,11). Because hexamerins have well defined roles as JH-binding proteins (19,20), because of the well established role of JH in termite caste differentiation (15), and on the basis of our observations that one of the hexamerins (Hex-2) is highly induced in response to rising JH titers during presoldier differentiation (11), we sought to further functionally characterize the Reticulitermes flavipes hexamerins. Here, our goal was to use RNA interference (RNAi) to investigate the roles of these two hexamerins in soldier caste differentiation by worker termites.…”

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confidence: 99%

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Social exploitation of hexamerin: RNAi reveals a major caste-regulatory factor in termites

Zhou

Scharf

2006

Proc. Natl. Acad. Sci. U.S.A.

221

211

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Lower termites express a unique form of eusocial polyphenism in that totipotent workers can differentiate into either soldier or reproductive caste phenotypes. In this initial effort using RNA interference in termites, we found that two hexamerin genes, Hex-1 and Hex-2, participate in the regulation of caste polyphenism. Our methodology involved a dual gene-silencing approach that used a single short-interfering RNA fragment to silence the two homologous hexamerin genes. We performed validation studies that evaluated effects on nontarget housekeeping genes, silencing of a nonhousekeeping control gene, and effects at the protein level. We found that the two hexamerin proteins, which are inducible by the morphogenetic juvenile hormone and which constitute a significant proportion of total termite protein, suppress juvenile-hormone-dependent worker differentiation to the soldier caste phenotype. This mechanism allows termite colonies to retain high proportions of altruistic worker caste members, thus apparently enhancing colony-inclusive fitness. These findings demonstrate a unique status quo regulatory mechanism for termite worker caste retention and provide an example of previously undescribed preadult developmental͞caste-regulatory genes from any social insect.sociogenomics ͉ RNA interference ͉ short-interfering RNA ͉ juvenile hormone ͉ phenotypic plasticity

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Section: Effects Of Rnai On Hexamerin Protein Expressionmentioning

confidence: 77%

Section: Effects Of Rnai On Hexamerin Protein Expressionmentioning

confidence: 99%

mentioning

confidence: 99%

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Social exploitation of hexamerin: RNAi reveals a major caste-regulatory factor in termites

Zhou

Scharf

2006

Proc. Natl. Acad. Sci. U.S.A.

221

211

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“…12,32,33) The major functions of JHBP that have been hypothesized are to transport JH in the hemolymph, to protect JH from the degradation by hemolymph enzymes, and to facilitate JH recognition and uptake by target cells. Three classes of hemolymph JHBP-(1) low-molecular-weight JHBP, (2) high-molecular-weight JHBP (lipophorins) and (3) high-molecular-weight hexameric JHBP 34) -have been characterized in different insect groups. 33,35) The JH-binding site in the low-molecular-weight JHBP was mapped using a photoaffinity analog of JH II, 36) but the analysis of the three-dimensional structure of JHBP is still in progress.…”

Section: Biosynthesis Transport and Metabolism Of Juvenile Hormonementioning

confidence: 99%

Insect juvenile hormone action as a potential target of pest management

Minakuchi

Riddiford

2006

J. Pestic. Sci.

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Juvenile hormone (JH) is a sesquiterpenoid hormone that regulates growth and development in insects. Since JH is a hormone specific to insects and other arthropods, compounds disrupting JH action in insects are expected to be ideal insecticides with low toxicity to non-target organisms. Many natural or synthetic analogs with JH-like or anti-JH activity have been identified, and some potent JH mimics have been used as insecticides. Recent studies on the enzymes in JH biosynthetic and metabolic pathways should be helpful for the discovery of more potent analogs and for the establishment of new means of pest management using recombinant DNA technology. © Pesticide Science Society of Japan Keywords: juvenile hormone (JH), insect metamorphosis, insect growth regulators, biosynthesis and metabolism of JH. Review* To whom correspondence should be addressed. E-mail: chieka_minakuchi@yahoo.com © Pesticide Science Society of Japan doptera. 17,18) Higher Diptera such as D. melanogaster and the blowfly Calliphora vomitoria produce JH III bisepoxide. 19,20) A small amount of methyl farnesoate, a precursor of JH III, was found in cockroach embryos and larvae. [20][21][22] Methyl farnesoate has also been identified in crustaceans 23) and is thought to have a JH-like action in female reproduction. 24)12Ј-OH JH III identified from the corpora allata of the African locust Locusta migratoria migratorioides was reported to exhibit JH activity when a high dose of this compound was topically applied to Tenebrio pupae. 25,26) Biosynthesis, Transport and Metabolism of Juvenile HormoneIn insects, JH is synthesized in the corpora allata via the mevalonate pathway (Fig. 2).27) The mevalonate pathway also exists in mammals and plants, and the early steps from acetylCoA to farnesyl diphosphate are conserved among these organisms. Importantly, insects and other arthropods do not synthesize cholesterol de novo but have to acquire it from dietary sources because they lack the genes encoding squalene synthase and other subsequent enzymes of the sterol branch. 28,29) Another peculiarity of the mevalonate pathway in insects is the capacity to synthesize JH via the isoprenoid branch.The genes encoding the enzymes in the mevalonate pathway from acetyl-CoA to farnesyl diphosphate have been identified in the genome of D. melanogaster and the malaria mosquito Anopheles gambiae, and in an EST library of the pine engraver Ips pini.27) However, it has been difficult to identify the genes encoding enzymes from farnesyl diphosphate to JH

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“…Analyzing the binding pocket, one might think that other hydrophobic metabolic compounds can be bound as well. Braun and Wyatt (25) reported that the hydrophobic juvenile hormone is bound by a serum protein belonging to the protein family of hexamerins with an affinity that is more than 5 orders of magnitude higher. The observation of the authors that this hexamerin looses the binding capacity when the N-terminal 53 amino acids are removed supports our hypothesis that the first domain could serve as a binding site for hydrophobic compounds.…”

Section: Figmentioning

confidence: 99%

Spider Hemocyanin Binds Ecdysone and 20-OH-Ecdysone

Jaenicke¹,

Föll²,

Decker³

1999

Journal of Biological Chemistry

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Sequence of the Hexameric Juvenile Hormone-binding Protein from the Hemolymph of Locusta migratoria

Abstract: The cDNA for the hexameric hemolymph juvenile hormone-binding protein (JHBP) from the migratory locust has been cloned and sequenced. Antiserum raised against purified JHBP was used to identify clones in an expression library.

Cited by 88 publications

References 42 publications

Social exploitation of hexamerin: RNAi reveals a major caste-regulatory factor in termites

Social exploitation of hexamerin: RNAi reveals a major caste-regulatory factor in termites

Insect juvenile hormone action as a potential target of pest management

Spider Hemocyanin Binds Ecdysone and 20-OH-Ecdysone

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