Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F22%3A00564648" target="_blank" >RIV/60077344:_____/22:00564648 - isvavai.cz</a>

Alternative codes found

RIV/68378050:_____/22:00564648 RIV/60076658:12310/22:43905125

Result on the web

<a href="https://www.frontiersin.org/articles/10.3389/fmolb.2022.1023381/pdf" target="_blank" >https://www.frontiersin.org/articles/10.3389/fmolb.2022.1023381/pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fmolb.2022.1023381" target="_blank" >10.3389/fmolb.2022.1023381</a>

Result language

angličtina

Original language name

Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains

Original language description

Silk is a secretory product of numerous arthropods with remarkable mechanical properties. In this work, we present the complete sequences of the putative major silk proteins of E. kuehniella and compare them with those of G. mellonella, which belongs to the same moth family Pyralidae. To identify the silk genes of both species, we combined proteomic analysis of cocoon silk with a homology search in transcriptomes and genomic sequences to complement the information on both species. We analyzed structure of the candidate genes obtained, their expression specificity and their evolutionary relationships. We demonstrate that the silks of E. kuehniella and G. mellonella differ in their hydrophobicity and that the silk of E. kuehniella is highly hygroscopic. In our experiments, we show that the number of genes encoding sericins is higher in G. mellonella than in E. kuehniella. By analyzing the synteny of the chromosomal segment encoding sericin genes in both moth species, we found that the region encoding sericins is duplicated in G. mellonella. Finally, we present the complete primary structures of nine fibH genes and proteins from both families of the suborder Pyraloidea and discuss their specific and conserved features. This study provides a foundation for future research on the evolution of silk proteins and lays the groundwork for future detailed functional studies.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10605 - Developmental biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Frontiers in molecular biosciences

ISSN

2296-889X

e-ISSN

2296-889X

Volume of the periodical

9

Issue of the periodical within the volume

NOV 29

Country of publishing house

CH - SWITZERLAND

Number of pages

16

Pages from-to

1023381

UT code for WoS article

000898484800001

EID of the result in the Scopus database

2-s2.0-85143895901