Complete nucleotide sequence of the gene encoding the<i>Bombyx mori</i>silk protein P25 and predicted amino acid sequence of the protein

Chevillard, Martine; Couble, Pierre; Prudhomme, Jean-Claude

doi:10.1093/nar/14.15.6341

Cited by 53 publications

(45 citation statements)

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“…4) Deduced amino acid sequences of P25s between B. mori and B. mandarina differ in only one residue (Q or R) at position 62, which was caused by a single base change (CAG or CGG). 4,5,11,12) It is noted that there is one discrepancy between the B. mori P25 sequence in the database (SWISS-PROT: P04148; NCBInr: A25513) and the sequence reported previously. 5,11,12) In the database, there is another residue (Q or H) difference at the site of 219 between B. mori P25 and B. mandarina P25.…”

Section: Discussionmentioning

confidence: 92%

“…4,5,11,12) It is noted that there is one discrepancy between the B. mori P25 sequence in the database (SWISS-PROT: P04148; NCBInr: A25513) and the sequence reported previously. 5,11,12) In the database, there is another residue (Q or H) difference at the site of 219 between B. mori P25 and B. mandarina P25. We carried out a comparison of peptide mass fingerprinting analysis of the database B. mori P25 with that of the reported B. mori P25 sequence, using the MSdigest analysis tool on the ExpPASy server to cleave the P25 sequences.…”

Section: Discussionmentioning

confidence: 92%

“…Based on the results of 2-DE and MALDI-TOF MS, we confirmed that the difference in sequences between B. mori P25 and B. mandarina P25 is a single amino acid substitution. The P25 gene was elucidated not only in B. mori [11][12][13] but also in B. mandarina. 4) Deduced amino acid sequences of P25s between B. mori and B. mandarina differ in only one residue (Q or R) at position 62, which was caused by a single base change (CAG or CGG).…”

Section: Discussionmentioning

confidence: 99%

“…No significant difference existed in the results of identification. So the reported B. mori P25 sequence 5,11,12) was used in the identification and dephosphorylation analysis.…”

Section: Discussionmentioning

confidence: 99%

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Proteomic Studies of Isoforms of the P25 Component ofBombyx moriFibroin

Zhang¹,

Yamamoto²,

Aso³

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

“…No significant difference existed in the results of identification. So the reported B. mori P25 sequence 5,11,12) was used in the identification and dephosphorylation analysis.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Proteomic Studies of Isoforms of the P25 Component ofBombyx moriFibroin

Zhang¹,

Yamamoto²,

Aso³

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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“…One set of these silk gland-specific genes with remarkable characteristics of expression is the two genes coding for the silk proteins P25 and fibroin (5,31), two abundant silk proteins of the cocoon (6,24). P25 and fibroin gene expression is characterized by a restricted territorial specificity, since it occurs only in the -500 cells of the posterior silk gland (PSG); the cells in the median silk gland (MSG) express another set of genes, encoding the so-called sericin proteins (10).…”

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confidence: 99%

P25 gene regulation in Bombyx mori silk gland: two promoter-binding factors have distinct tissue and developmental specificities.

Durand¹,

Drevet²,

Couble³

1992

Mol. Cell. Biol.

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The gene encoding the silk protein P25 is expressed in the posterior silk gland of Bombyx mori with strict territorial and developmental specificities. The cis-acting regulatory elements previously located within the 441-bp 5' proximal sequence of the gene were examined for protein-binding capacities. We identified two factors, BMFA and SGFB, that lead to prominent band shifts and the target sites for which are included in a region homologous to the fibroin gene enhancer sequence. Analysis of the tissue-specific incidence of both factors showed that BMFA is ubiquitous, whereas SGFB is restricted to the silk gland cells. However, SGFB was found in both posterior and middle silk gland cells and therefore likely directs organ-specific, but not territory-specific, expression. Developmental studies throughout the fourth larval molt, at which the P25 gene status changes from derepressed to repressed, revealed that BMFA is reversibly modified at the transition from intermolt to molt. Indeed, the preexisting BMFA is replaced by a structurally related factor, BMFA', during the 2 h following head capsule apolysis. The exact temporal coincidence of this conversion with the onset of gene repression suggests that BMFA' is involved in transcription inactivation and likely results from a transduction process initiated by the hormonal change at molting.

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Silk‐Based Biomaterials

Gomes¹,

Leonor²,

Mano³

et al. 2012

Biomimetic Approaches for Biomaterials Development

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IntroductionSilk is a hierarchically structured fibrous protein that has been used for thousands of years for different applications such as textile production and wound dressings [1]. Although silk proteins are produced by a large number of arthropod species such as wasps, bees, and crickets, during the past few decades, the scientific community has focused its attention in the silk produced by the mulberry silkworm Bombyx mori and by different spider species. Farming of the silkworm B. mori started around 5000 years ago in China, and since then, the cocoon case produced by this animal has been used as a source of silk for the textile industry. More recently, B. mori silk has been used commercially in the development of sutures for medical applications [1,2]. In contrast to B. mori silk, spider silk has not been commercialized for biomedical proposes mainly because of the territorial cannibalistic behavior of spiders, which makes them difficult to farm, along with the low levels of silk production. However, in the past, spider webs have been used as bandages for wound dressing, because of its antimicrobial properties, and in other human activities such as fishing and hunting [3]. The results from recent studies demonstrating the biocompatibility of silk and the exquisite mechanical properties of silk fibers, especially in the case of spider silk, are the main reasons why B. mori and spider silk proteins have been the target of intense research efforts, when compared with the silk produced by other arthropods, aimed at developing new silk-based biomaterials with superior mechanical and biological properties.On the basis of the background given above and since B. mori and spider silk are the most extensively characterized silk, this chapter focuses on the silk proteins produced by these animals and on the perspectives of using these proteins for future biomedical applications.The silk produced by B. mori is the most widely used, since this silkworm is easy to farm, allowing for steady and large-scale production [1]. The B. mori silk fiber is formed by two microfilaments embedded in a gluelike glycoprotein named sericin, which works as a coating and is used by the animal for cocoon assembly. Each microfilament results from the assembly of a hydrophobic ∼370 kDa heavy-chain fibroin protein, with a relatively hydrophilic ∼25 kDa light-chain fibroin and a 30 kDa P25 protein [4]. The heavy-chain fibroin is a large insoluble macromolecule formed by ∼5263 amino acids and is rich in glycine (G, 45.9%), alanine (A, 30.3%), serine (S, 12.2%), tyrosine (Y, 5.3%), and valine (V, 1.8%) residues [1,5]. This heavy-chain fibroin is formed by a highly repetitive crystalline fraction of 2377 repeats of GX. The X position is occupied by the A residue in 64% of the repeats, by S in 22%, by Y in 10%, by V in 3%, and by threonine (T) in 1.3% of the repeats [5,6]. These repetitive cores form 12 domains that alternate with 11 nonrepetitive amorphous domains formed by 25 amino acids residues, which connect the crystalline domains. These a...

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Complete nucleotide sequence of the gene encoding theBombyx morisilk protein P25 and predicted amino acid sequence of the protein

Cited by 53 publications

References 1 publication

Proteomic Studies of Isoforms of the P25 Component ofBombyx moriFibroin

Proteomic Studies of Isoforms of the P25 Component ofBombyx moriFibroin

P25 gene regulation in Bombyx mori silk gland: two promoter-binding factors have distinct tissue and developmental specificities.

Silk‐Based Biomaterials

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