Sericin composition in the silk of Antheraea yamamai
Publication in Biomacromolecules describes five sericin genes from a wild silkmoth, A. yamamai; provides whole gene structures and assigns them to major sericin proteins extracted from A. yamamai cocoon.
The silks produced by caterpillars consist of fibroin proteins that form a pair of core filaments, and sericin proteins that seal filaments into a fiber and conglutinate fibers in the cocoon. Although silk is an important class of natural polymers for materials development, our knowledge on silk sericin proteins is limited. We analyzed a transcriptome based on the Antheraea yamamai silk glands and annotated assembled contigs to diverse functional groups. Sericin cDNAs were identified based on similarity to the known sericin genes from B. mori and G. melonella. In addition, we assigned respective contigs to the main silk proteins from the A. yamamai cocoon separated by PAGE, and followed by mass spectroscopy or N-terminal sequencing. We demonstrate that there are five sericin genes in A. yamamai, which are very different from the three known sericin genes of B. mori. The A. yamamai sericin genes produce transcripts of 3.5 – 5.4 kb, coding for proteins with central repetitive region(s) and high contents of Ser and charged amino acid residues. Accurate sequence information on A. yamamai sericin provided in this publication will be an important clue to understand the function and evolution of sericins in silk formation.
Žurovec M., Yonemura N., Kludkiewicz B., Sehnal F., Kodrík D., Marques Cota Vieira L., Kučerová L., Strnad H., Koník P., Sehadová H. (2016) Sericin Composition in the Silk of Antheraea yamamai. Biomacromolecules DOI: 10.1021/acs.biomac.6b00189
