On the origin of the yolk protein ferritin in snails

Bottke, Werner; Burschyk, Monika; Volmer, Jutta

doi:10.1007/bf00398988

Cited by 22 publications

(25 citation statements)

References 21 publications

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“…Ferretin containing proteins have also been shown to be associated with early shell deposition in gastropod larvae, and are present here (Zhang et al., ). Yolk ferretin was also highly expressed in viable embryos, and is likely related to gut development and embryonic nutrition as transcripts have been shown to localize to the developing gut of the freshwater snail Lymnaea stagnalis (Bottke et al., ). Another transcript that is likely involved in gut differentiation is cathepsin B.…”

Section: Resultsmentioning

confidence: 99%

Comparative Transcriptomics of Alternative Developmental Phenotypes in a Marine Gastropod

2016

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Alternative phenotypes are discrete phenotypic differences that develop in response to both genetic and environmental cues. Nutritive embryos, which arrest their development to serve as nutrition for their viable siblings, are an example of an alternative developmental phenotype found in many animal groups. Females of the marine snail, Crepidula navicella, produce broods that consist mainly of nutritive embryos and a small number of viable embryos. In order to better understand the genetic mechanisms that lead to the development of alternative phenotypes in this species, we compared the transcriptomes of viable and nutritive embryos at the earliest stage that we were able to distinguish visually between the two. Using high-throughput Illumina sequencing, we assembled and annotated a de novo transcriptome and compared transcript levels in viable and nutritive embryos. Viable embryos express high levels of transcripts associated with known developmental events, while nutritive embryos express high levels of apoptosis-related transcripts. Gene Ontology term enrichment with GOSeq found that these are associated with the negative regulation of apoptotic processes. This enrichment, combined with morphological evidence, suggests that apoptosis is important in the formation of gastrula-like nutritive embryos. Apoptosis has been implicated in the development of alternative phenotypes in other animal groups, raising the possibility that this mechanism's role in alternative phenotypes is conserved in gastropod development. We suggest possible alternative mechanisms of nutritive embryo development. Most importantly, we contribute further evidence to the hypothesis that nutritive embryos are an alternative developmental phenotype.

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Section: Resultsmentioning

confidence: 99%

Comparative Transcriptomics of Alternative Developmental Phenotypes in a Marine Gastropod

2016

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“…Vitellogenin, also a pluripotent protein, is the precursor of the lipoproteins and phosphoproteins that make up yolk protein, which may also provide more efficient nutrition for the embryos (73). Ferritin, the iron storage protein, has a similar nutritive role as yolk protein (74). Therefore, these proteins may work together as either a nutrition reservoir or as development promoters that ensure the growth of young embryos.…”

Section: Proteins Expressed By 24h Embryos Play Key Roles In Nutritiomentioning

confidence: 99%

In-depth Proteomics Characterization of Embryogenesis of the Honey Bee Worker (Apis mellifera ligustica)

Mao

Han

et al. 2014

Molecular & Cellular Proteomics

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Identifying proteome changes of honey bee embryogenesis is of prime importance for unraveling the molecular mechanisms that they underlie. However, many proteomic changes during the embryonic period are not well characterized. We analyzed the proteomic alterations over the complete time course of honey bee worker embryogenesis at 24, 48, and 72 h of age, using mass spectrometry-based proteomics, label-free quantitation, and bioinformatics. Of the 1460 proteins identified the embryo of all three ages, the core proteome (proteins shared by the embryos of all three ages, accounting for 40%) was mainly involved in protein synthesis, metabolic energy, development, and molecular transporter, which indicates their centrality in driving embryogenesis. However, embryos at different developmental stages have their own specific proteome and pathway signatures to coordinate and modulate developmental events. The young embryos (<24 h) stronger expression of proteins related to nutrition storage and nucleic acid metabolism may correlate with the cell proliferation occurring at this stage. The middle aged embryos (24 -48 h) enhanced expression of proteins associated with cell cycle control, transporters, antioxidant activity, and the cytoskeleton suggest their roles to support rudimentary organogenesis. Among these proteins, the biological pathways of aminoacyl-tRNA biosynthesis, ␤-alanine metabolism, and protein export are intensively activated in the embryos of middle age. The old embryos (48 -72 h) elevated expression of proteins implicated in fatty acid metabolism and morphogenesis indicate their functionality for the formation and development of organs and dorsal closure, in which the biological pathways of fatty acid metabolism and RNA transport are highly activated. These findings add novel understanding to the molecular details of honey bee embryogenesis, in which the programmed activation of the proteome matches with the physiological transition observed during embryogenesis. The identified biological pathways and key node proteins allow for further functional analysis and genetic manipulation for both the honey bee embryos and other eusocial insects. Molecular & Cellular Proteomics 13:

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“…Yolk ferritin is a secreted ferritin (Bottke et al, 1988) which is synthesized as a preprotein. This suggests that transfer of the subunit across the membrane of the endoplasmic reticulum may be a critical step for attaining the correctly folded state as essential for assembly into the multimeric apoferritin shell.…”

Section: Over-expression Of Yolk Ferritin In E Coli Dhwpmal-pamentioning

confidence: 99%

Expression in Escherichia coli of a secreted invertebrate ferritin

Darl

Harrison

Bottke

1994

European Journal of Biochemistry

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The coding regions of the cDNAs for cytoplasmic soma ferritin and secreted yolk ferritin from the snail Lymnaea stagnalis were inserted into the prokaryotic expression vector pEMBLex2. The vector directed the synthesis in Escherichia coli of soma ferritin up to a concentration of 15% of soluble proteins. Soma ferritin was expressed as the multimeric protein (480 kDa). Its similarity with natural soma ferritin was confirmed by PAGE, immunostaining and electron microscopy. Yolk ferritin was expressed in the form of inclusion bodies. Attempts to refold and assemble the purified yolk ferritin subunit in vitro failed. The yolk ferritin coding sequence was therefore inserted into the expression vector pMAL-p2.At a growth temperature of the bacterial cells of 23 "C and at an isopropyl P-D-thiogalactopyranoside concentration of 50 pM, about 5% of the induced MalE-yolk-ferritin fusion protein was secreted into the periplasmic space and could be purified by affinity chromatography on amylose; the rest occurred as insoluble cytoplasmic inclusion bodies. Soluble MalE -yolk-ferritin fusion protein was capable of assembly into ferritin-like particles. Fully assembled yolk apoferritin shells (610 kDa) were obtained by digestion of these particles with proteinase K (yield: 180 pg yolk ferritidl bacterial culture). Recombinant yolk ferritin was capable of taking up iron in vitro. Yolk ferritin (610 kDa) and soma ferritin (480 kDa) were run to the pore limit of a non-denaturing 5-20% PAGE gradient gel. Under these conditions, yolk ferritin had a higher mobility than soma ferritin (480 kDa) and therefore the yolk ferritin may have a rather compact structure. A 41-aminoacid-residue stretch of the insertion, a distinctive feature of the yolk ferritin subunit, was deleted by site-directed mutagenesis. The MalE-yolk-ferritin variant thus obtained was readily degradable by proteinase K and could not be assembled into ferritin-like particles. Therefore residues in the deleted peptide must be important for the maintenance of the native structure.Iron is an essential element for virtually all forms of life, being a constituent of many proteins involved in fundamental processes such as respiration, photosynthesis, nitrogen fixation, DNA synthesis and cell division. Sequestration of iron in a soluble, nontoxic and bio-available form is achieved by ferritins, a class of proteins which are widely distributed among prokaryotes and eukaryotes and which are capable of storing up to 4500 iron atoms/molecule inside their protein coats. Structure, function and regulation of ferritins have been intensively investigated (reviewed by Theil, 1987 ;Harrison et al., 1989Harrison et al., , 1991 Andrews et al., 1992). X-ray crystallographic analyses of both naturally occurring ferritins from vertebrates and recombinant ferritins from vertebrates and an invertebrate species revealed a remarkable conservation of three-dimensional structure (Harrison et al. 1991). Recent results from sequencing of plant ferritin cDNAs and computerassisted model-building sugge...

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On the origin of the yolk protein ferritin in snails

Cited by 22 publications

References 21 publications

Comparative Transcriptomics of Alternative Developmental Phenotypes in a Marine Gastropod

Comparative Transcriptomics of Alternative Developmental Phenotypes in a Marine Gastropod

In-depth Proteomics Characterization of Embryogenesis of the Honey Bee Worker (Apis mellifera ligustica)

Expression in Escherichia coli of a secreted invertebrate ferritin

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