Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the Ser 1B cDNA

Garel, Annie; Deléage, Gilbert; Prudhomme, Jean-Claude

doi:10.1016/s0965-1748(97)00022-2

Cited by 131 publications

(113 citation statements)

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“…One relates to the correspondences of the three polypeptides to sericin genes: sericins1 deduced from the Ser1 gene 8) showed the same characteristics as sericins M and P, and S-2 polypeptide produced by the Src-2 gene 13) was very similar to sericin A (Table 1, Ser1C is one of sericins1), when attention was focused on the contents of glutamic acid containing glutamine, threonine, lysine, and tyrosine. This suggests the possibilities that sericins M and P are the products of the Ser1 gene, and that sericin A is identical to the S-2 polypeptide produced by the Src-2 gene.…”

Section: )mentioning

confidence: 99%

“…7) Recent studies on sericin genes provided further information about the constituents of sericin. The Ser1 gene was reported to produce mRNAs with sizes of 10.5, 9.0, 4.0, and 2.8 kb by alternative splicing, 8) and the Ser2 gene was found to produce mRNAs with sizes of 6.4 or 5.0 and 3.1 kb. 9) In spite of these studies, we have not reached a consensus about the constitution of sericin, and especially, there has been no attempt to estimate sericin components quantitatively.…”

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confidence: 99%

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Isolation of Three Main Sericin Components from the Cocoon of the Silkworm,Bombyx mori

Takasu

Yamada

Tsubouchi

2002

Bioscience, Biotechnology, and Biochemistry

269

202

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Section: )mentioning

confidence: 99%

mentioning

confidence: 99%

Isolation of Three Main Sericin Components from the Cocoon of the Silkworm,Bombyx mori

Takasu

Yamada

Tsubouchi

2002

Bioscience, Biotechnology, and Biochemistry

269

202

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“…Two genes encode sericins, Ser1 and Ser2 (5)(6)(7)(8). The different molecular weight sericins are the products of different splicing events at the transcript level.…”

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confidence: 99%

Cloning, Expression, and Assembly of Sericin-like Protein

Huang

Valluzzi

Bini

et al. 2003

Journal of Biological Chemistry

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Recombinant sericin proteins of different molecular masses (17.4, 31.9, and 46.5 kDa), based on the 38-amino acid repetitive motif of native sericin, were cloned, expressed, and purified. The recombinant sericin self-assembled during dialysis (starting concentration of 2.5 mg/ml) forming twisted fibers. Circular dichroism and Fourier transform infrared spectroscopy studies demonstrated protein conformational transitions occurred from random coil to ␤-sheets during the dialysis. Congo red-stained recombinant sericin fibrils exhibited applegreen birefringence, indicating long-range order in the array of ␤-sheets. Biosynthetic sericin has a high content of polar amino acids (e.g. Silk of Bombyx mori is composed of two kinds of proteins: the fibroin which is synthesized in the posterior silk gland and the sericins produced by the middle silk gland. The sericins bind two fibroin fibers together in the anterior region of the gland as the fibers are spun to form the cocoon. Sericins represent a family of proteins whose molecular mass ranges from 20 to 310 kDa (2, 3) and are characterized by an unusually high serine content, 38.1 mol % (4). Sericins are soluble in hot water, which makes it possible to degum the silk fibroin threads.Two genes encode sericins, Ser1 and Ser2 (5-8). The different molecular weight sericins are the products of different splicing events at the transcript level. Some conformation studies with sericins from the silk gland of B. mori or regenerated sericin from B. mori cocoons suggested random coil with some ␤ structure (9, 10). However, the samples used in these studies were mixtures of the various native sericin proteins, therefore the structure of the individual proteins is unknown and the contribution of specific sequences toward secondary structure is not confirmed. Sericin model peptides such as poly(L-serine) (11-16), poly(O-benzyl-L-serine) (12), and poly(O-acetyl-L-serine) (13,14) were synthesized for structural feature characterization. The ability of poly(L-serine) to fold into a ␤ conformation depended on molecular weight. Low molecular weight poly(L-serine) (molecular weight 650) was soluble and adopted a random coil conformation in aqueous solution, whereas high molecular weight poly(L-serine) (molecular weight 105,000) formed ␤-sheets and was insoluble in water (11). However, homopolypeptides like poly(L-serine) do not match native sericin in terms of amino acid composition, sequence, and molecular weight. Therefore, to better understand sericin structure, interactions between sericin and fibroin, and the biological relevance of sericin in fiber structure, high molecular weight pure sericin-like proteins are required.Sericin 1 encoded by Ser 1 consists of 70 repeats of the 38-amino acid motif (5): SSTGSSSNTDSNSNSVGSSTS-GGSSTYGYSSNSRDGSV. The molecular mass of sericin 1 proteins is 76 -284 kDa. The 38-amino acid repeat motif exhibits a high content of hydrophilic amino acids: 44.7% serine, 10.5% threonine, and 7.9% tyrosine, very close to the average amino acid composition of serici...

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“…As for the other sericin fractions, it seems difficult to be removed thoroughly although those fractions are still more hydrophilic than fibroin fraction. It has been reported previously that those sericin fractions tend to aggregate each other and will form stable beta sheet structure [16,18]. In the formation of beta sheet structure among extended sericin chains it has been pointed out that Ser and Thr linkage sequences are responsible for the formation of beta sheet [19].…”

Section: Structure Of Liquid Silk Membranementioning

confidence: 99%

<b>Separation of Ethanol-Water Mixtures by the Membranes Prepared from Liquid Silk</b>

Kawahara¹,

Ito²

2014

Sen-i Gakkaishi

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Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the Ser 1B cDNA

Cited by 131 publications

References 15 publications

Isolation of Three Main Sericin Components from the Cocoon of the Silkworm,Bombyx mori

Isolation of Three Main Sericin Components from the Cocoon of the Silkworm,Bombyx mori

Cloning, Expression, and Assembly of Sericin-like Protein

<b>Separation of Ethanol-Water Mixtures by the Membranes Prepared from Liquid Silk</b>

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